The Consequences Of Cheese As A Main Source Of Protein

InChristAlone

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The following words have nothing to do with the fact that desalting cheeses immersing in tap wasser is not as effective as sprint wasser: chlorinidization makes it harder to pull the salt from it.

But I digest.

B12

From praevious pages, it was estimated that the ratio of B12 (mcg) to methionine (mg) is about:

5.0:1 for steak
4.3:1 for milk
1.6:1 for cheese​

I guess for meats and cheeses it can vary more than milk.

For B12, it's unlikely that people will be consuming other food sources to compensate in the same meal. The body can resort to reserves (tut) but this isn't good if the person already has an insufficiency. B12 deficiency might not be due to its lack in the diet, but either way, casein full-force will deplete the person further.

I suspect it's possible for cultures to remain healthy for a very long time, eating meats only on rare occasions, and not have problems as long as the methionid content of the diet is frequently low.

A food that's high in methionine but reduced in its B12 content will accelerate the vitamin depletion. This might be another contributor to the constipating effect of cheese: to extract most of its B12 and avoid problems with methionine metabolism, which (according to the original post) happens after 5 hours after the meal, the peak in blood homocysteid.

Gelatin can mitigate some of these problems as long as you can do something useful with homocysteine. It must be methylated to methionine again or be used for synthesizing cysteine. So either way, it works best if the diet is providing an abundance of other B-vitamins.
If you're deficient in choline for example, the production in the body requires methyl groups from methionine. It doesn't make sense to recycle homocysteine using betaine if you're already deficient in choline. So this can strain the recycling dependent on folate/B12, so their needs might be increased.

Heavier cheeses not only have less protein for the same weight, but also (based on the first post) retain more B12. This can ease the problems of refinement if the person is depleted. Cottage cheese in this regard is worse.

But what was really worse was the B6 loss in low-fat cottage cheese. If you note, the best food sources tend to be animal foods.
There are exceptions: bananas, dates, watermelons, figs, pineapfel, etc;
and in case the person eats cheese with salads: leafy greens, potatoes, etc.

Perhaps a little extra is desirable since B6 will be very-much needed to do something useful with homocysteine:

VitaleTherapeutics
The Effect of Soy Protein on Homocysteine

"Caseid is a fractionated milk protein product with elevated methionine levels and extremely low levels of the amino acid cysteine. This stimulates the body to make cysteine through the toxic intermediary homocysteine."

"Casein is a poor protein (tut) high in methionine and low in cysteine. Soy is a poor protein low in methionine and higher in cysteine. The fact that soy protein does not have a consistently and demonstrably better effect on homocysteine levels compared to casein indicates that it is a very poor quality protein indeed."

"In [a given study], soy performed even worse than the casein control in a variety of categories, including homocysteine."

"Rather than improve homocysteine levels, methionine deficiencies can lead to reduced SAM (s-adenosyl methionine) synthesis, which, in turn, might raise levels of homocysteine.[16] Diets containing soy protein isolates proved atherogenic to Cebus monkeys, but feeding supplemental methionine to them prevented atherogenesis, probably because of reduced plasma levels of homocysteine due to increased SAM synthesis.[15,16]"

"Soy protein is also likely to raise homocysteine levels because the cysteine is either biounavailable or damaged by modern processing methods. Much of the cysteine contained in soybeans is bound up in the cysteine protease inhibitors, which include the trypsin inhibitors, cystatins and soyacystatins. Because protease inhibitors are stubbornly resistant to heat treatments and other modern processing methods, soybean cysteine is not readily available compared to other proteins.[17-26] Compounding the problem, polyunsaturated oil residues leftover from the soy protein extraction processes create epoxides that are not only capable of poisoning L-cysteine but all other thiol substances in the body.[27-30] Cysteine itself can be rapidly oxidized and irreparably damaged during the manufacturing process when exposed to atmospheric oxygen and an alkaline pH (above about 7.5 to 8)[31] With such damage through treatments and exposures, it is not surprising that soy is such a poor source of cysteine."

"Cysteine is also damaged by chemical processing at high temperatures and intense pressures used to eliminate soy's beany flavor (which does not appeal to most consumers) and inactivate the antinutritional factors such as oligosaccharides and protease inhibitors (which cause flatulence and other forms of digestive distress).[32-35]"

"It has been known for decades that whenever the body attempts to replace depleted or unavailable levels of cysteine, it does so even if from limiting amounts of methionine, but mammalian systems do so through the toxic intermediary metabolite, homocysteine."

"Accumulated metal toxins in the body from the processing of foods and environmental exposures can contribute to failure of this pathway by binding and interfering with homocysteine's conversion, thereby causing it to accumulate metabolically.[38,39] Accumulating metal toxins may even co-precipitate with and concentrate homocysteine in vulnerable areas of the body causing arterial plaque, neoplasia, tumors and a variety of other metabolic imbalances.[40] The metals known to bind thiols the most tightly include some of the most potent known carcinogens. However, copper, iron, manganese and other metals that are nutritious or otherwise beneficial to the body in small amounts are also associated with cancer and other diseases when found at excessive levels and co-accumulating with homocysteine.[41,42]"

"Recently, a new, related threat has emerged. With the extensive use of antibiotics, resistant pathogenic organisms have developed. Several pathogens have been reported to divert methyl groups in order to methylate mercury or other toxic metals. When methylated, mercury is far more toxic, has far greater affinity for fatty tissues and is far more difficult to remove from the body.[43-45] Under normal circumstances, the body would use these methyl groups to regenerate methionine from homocysteine, to remove any inhibition of cysteine biochemistry by homocysteine, or to perform critical methylating reactions involving S-adenosyl-methionine (SAM).[46]"

"Yet another mechanism by which soy protein might increase homocysteine is through thyroid depression, a well-documented effect.[52-60] In addition to contributing to atherogenesis, arrhythmias, atrial fibrillation, PVCs and other heart disease risk markers, low thyroid status impacts homocysteine levels."

"Thyroid status influences the plasma tHcy. Free triiodothyronid and next free thyroxine have the greatest negative influence. This would account for hyperhomocysteinemia in the hypothyroid state and premature atherogenesis."

"[..]Hypothyroid subjects had higher total homocysteine in both genders[.] Hypothyroid females had higher total and LDL cholesterol, and were more often treated for diabetes."

"[..]soy protein is a product devoid of B12 and reportedly can even increase the body's requirements for B12. FDA-mandated B12 fortification might reduce soy protein's contribution to elevated homocysteine levels by providing the key nutrient (vitamin B12) required for converting it back to methionine, but fortification alone cannot make soy protein a “heart healthy” substance for the myriad reasons discussed above and elsewhere in this petition. These issues include but are not limited to the following: compromised availability of cysteine, cystine and methionine; the incomplete digestion of soy protein due to the action of protease inhibitors and other factors; and the toxic accumulations of ornithine and metal toxins which result from the processing of soy protein."​

Liver once a week does little in terms of making up for the B12 loss, unfortunately. According to the first post again, 2% cottage cheese loses 75% of its B12, so a gross simplification is to imagine that for every 4 meals with that cheese, 1 has the original B12 content and the other 3 are (as Travo would say) B12-null meals.

I guess the best compensation for the refinement is within the meal.
So for vegans is it mandatory to take a b12 supplement? I know there are some who say they didn't need one.
 
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Amazoniac

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So for vegans is it mandatory to take a b12 supplement? I know there are some who say they didn't need one.
I guess that most of the issues can be eased or prevented with B6 and folate, but..
High methionine intake without enough B12 is a very unusual thing for the body.
The problem is that people arrive here trying to improve some aspect of health, so an existing B12 deficiency isn't unlikely. And just like we commented elsewhere, regardless of the cause, brutalizing methionine won't help any: the body might be consuming its scarce reserves.
 

InChristAlone

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I guess that most of the issues can be eased or prevented with B6 and folate, but..

The problem is that people arrive here trying to improve some aspect of health, so an existing B12 deficiency isn't unlikely. And just like we commented elsewhere, regardless of the cause, brutalizing methionine won't help any: the body might be consuming its scarce reserves.
I guess that's why my body loves bananas. I always get over the RDA for b6 because of them.
 

lvysaur

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I've noticed the opioid-like effects of large quantities of milk. I totally eliminated it by switching to A2 milk.
 
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There's a problem in consuming a lot of methionine with way more calcium than magnesium: it can oppose a mineral that's already scarce, which is needed for correct metabolism of methionine (and almost everything else). Of course Chris has some interesting thoughts on it:

- https://www.westonaprice.org/helps-consider-magnesium-metabolic-rate/

"Here, I’d like to chip away at one small piece of the puzzle that I have not written about yet: why benefits from SAMe supplementation should cause one to look not only at the most commonly discussed methylation nutrients (e.g., B12, folate, choline, betaine, methionine) and genetic polymorphisms (e.g., MTHFR) but also at issues that are more commonly neglected when discussing methylation: magnesium and the metabolic rate."

"[..]before methionine can be used for methylation it must be activated to S-adenosyl-methione, which is sold as a supplement and in the supplement market generally abbreviated as SAMe."

"[..]any problems recycling methionine from homocysteine should be fully investigated because if these are the real problems then an expensive supplement like SAMe is a waste of money. These conditions would tend to be associated with elevated levels of homocysteine and they could include deficiencies of B12 or folate, especially in the context of a diet that is not rich in choline or betaine[.]"

"There is another possibility, however, that is strongly suggested by the biochemistry: some people may not be efficiently activating methionine to SAMe. In order for this activation to take place, the enzyme methionine adenosyltransferase (MAT, also known as S-adenosyl methionine synthetase) breaks apart ATP to harvest from it a molecule of adenosine and then activates methionine by sticking adenosine onto it."

"People who have severe genetic deficiencies of the MAT enzyme are unable to use methionine, even when adequately present, for the methylation process. This is because that methionine is never activated to SAMe. Thus, they are deficient in methylation, they have little risk of depleting glycine by consuming excess methionine if the problem isn’t fixed (though they still may have inadequate glycine for other purposes, such as detoxification and synthesizing collagen), and since they never use up the methionine to make homocysteine, their methionine becomes elevated rather than their homocysteine, and their homocysteine is actually low."

"The biochemistry suggests that people with a normally functioning MAT gene could have two other reasons for poor activation of methionine: poor magnesium status, or a low metabolic rate. Since ATP is the source of the activating molecule, the reaction is, quite clearly, ATP-dependent. Since ATP is always utilized as a chelate with magnesium, the reaction is also magnesium-dependent. The presence of a magnesium deficiency, a low metabolic rate, or both conditions together, could prevent methionine from being activated."

"It is important to realize, however, that a low metabolic rate or a magnesium deficiency will compromise thousands of bodily processes, and that either condition would be likely to coexist with multiple nutrient deficiencies. Thus, such a person will not necessarily replicate the presentation of someone with a genetic deficiency of the MAT enzyme. They will not, for example, necessarily have low homocysteine. If the recycling of homocysteine is also being compromised, then homocysteine could be normal or elevated even while methionine is failing to be utilized properly and is thereby generating homocysteine at a much lower rate."

"In my opinion, if someone benefits from SAMe supplementation or suffers from any of the conditions for which SAMe supplementation has shown to be beneficial, and it can be ruled out that simply ensuring adequacy of dietary methionine and relevant B vitamins would fix the problem, magnesium status and metabolic rate should be evaluated."

"Ensuring a normal basal body temperature is, in my current opinion, probably the most cost-effective and helpful way to address the metabolic rate. However, addressing why the metabolism may have slowed may be more complicated."​

- https://chrismasterjohnphd.com/2017/07/17/methylate-way-mental-health-dopamine/

"So first of all, the principal methyl donor for hundreds of different methylation reactions is S-adenosylmethionine. You take methionine, which is an amino acid that comes from your dietary protein and which is found in animal proteins and plant proteins but which is twice as abundant in animal proteins as it is in plant proteins—you take methionine, and then you activate it using magnesium and ATP. ATP is adenosine triphosphate. If you break apart the phosphates at the end, you get energy. But if you break all of them off, you get adenosine. And if you take that adenosine and you take that energy and you tack it onto the methionine molecule, you get S-adenosylmethionine. That requires ATP. Everything that requires ATP requires magnesium because ATP does everything it does as a chelate of magnesium."

"So once you have methionine in from your dietary protein and you activate it using magnesium and ATP, you have S-adenosylmethionine. Now, this—which is incidentally sold as a supplement as often colloquially called SAMe—this is the principal methyl donor that through hundreds of different reactions mediated by different enzymes that are all called some variation of a methyltransferase, you take this methyl group from S-adenosylmethionine, and you donate it to something else."

"If you have methionine, and you take away a methyl group—which incidentally is where methionine gets its name from: “meth-” from methyl group and “-thi-” coming from the Greek theîon, meaning sulfur, and this is because if you look at the methionine molecule, you would see that it’s one of the two amino acids that contains sulfur in it. The other one is cysteine, so it’s one of the two sulfur amino acids. And on the end of that sulfur, that sulfur is capped by a methyl group, and that’s the methyl group that you remove when you methylate things, like dopamine or precursors to creatine."

"Once you get rid of that methyl group, you would have homocysteine. But because you’re using S-adenosylmethionine, what you actually have left over is S-adenosylhomocysteine. You then hydrolyze the adenosyl group from that, meaning the adenosine from ATP that you stuck onto it, you now take off. With that, you can regenerate ATP in the system of energy metabolism."

"But now you have homocysteine, and homocysteine is normal to have, it’s important to have, it’s always a byproduct of this system. But many of you may know homocysteine as something that goes high when you have higher heart disease risk. So homocysteine is often measured in the blood for that reason. If your homocysteine is high, it’s taken as an indication that you have greater risk of heart disease, and that’s because homocysteine can cause oxidative stress and can damage blood vessels. But if we’re paying attention to how the system works, high homocysteine is probably more problematic simply as a result of this system being defective."

"So what do you do with that homocysteine? Well, there’s two principal fates of homocysteine. One is that if you have a lot of it, more than you need for methylation, you can turn it into cysteine using the help of vitamin B6 and of the amino acids serine or glycine. And with that cysteine, you can turn it into taurine or sulfate or glutathione.

Taurine is important for the electrical activity in the brain and retina. Sulfate is important for many things in regulating hormones and promoting detoxification and other uses. Glutathione is an antioxidant, in fact the central antioxidant of the cell, but also important in detoxification, it regulates hundreds of proteins, protects the lungs from oxidative stress, makes mucus fluid, does all kinds of great things like that. So if you have lots and lots and lots of homocysteine, you might be putting it into cysteine so it can go down through those pathways.

But the first thing you do with homocysteine, the regular thing you do with homocysteine, the thing that you’re pretty much always doing with homocysteine in between your meals when you didn’t just eat a huge methionine load from a steak, is you are recycling the homocysteine back to methionine.

Now, imagine that you ate this methionine from your steak or wherever it came from, you only used it once, and that methyl group is gone, so maybe you synthesized one molecule of creatine or part of a molecule of creatine, or you got rid of one molecule of dopamine. Whatever you did with that methyl group, the methyl group is now permanently gone.

So most of your methylation is actually coming from being able to recycle the homocysteine. How do you recycle it? Well, you have folate, which takes a methyl group from breaking down other amino acids and transferring it to vitamin B12. Vitamin B12 then transfers it to homocysteine. That sticks the methyl group back on the end of the molecule to cap that sulfur to get methionine, the methyl-capped sulfur amino acid. And once you do that, you can then activate it again using ATP and magnesium, and you get S-adenosylmethionine, and you can do another methylation cycle. Then you get homocysteine again, you gotta just do it over and over and over again.

Now, every time you recycle it, you are not consuming folate or B12. You’re simply consuming methyl groups that they are transferring. So you don’t need a molecule of folate to support one turn of the methylation cycle, but you need enough folate that you can keep the delivery of methyl groups going. You need enough B12 that you can keep the delivery of the methyl groups going. So if you don’t have incoming methyl groups from your amino acid metabolism, you can’t keep this system going. If you don’t have enough folate, you can’t keep it going. If you don’t have enough B12, you can’t keep it going.

Now, the system whereby folate gets its methyl group is actually really complicated, and I’m not gonna go into all the details, but I’ll say that your energy metabolism has to be working properly. You’re gonna have to have enough niacin, which is vitamin B3. You’re gonna have to have enough riboflavin, which is vitamin B2. You’re gonna have to have enough thiamin, which is vitamin B1. There’s various genetics that lie outside the methylation pathway that could impact this.

And of course, there’s famous genetics inside the methylation pathway that affect this. For example, MTHFR, that gene that really stands for 5,10-methylenetetrahydrofolate reductase, but you know what it looks like it means. I’m not marking this episode explicit, so I’m gonna skip that. You know what I’m talking about.

Anyway, the MTHFR gene is coding for the enzyme that does the final construction of the methyl group on folate. So if you have low MTHFR activity, then you are not gonna be able to get the methyl groups going through to homocysteine in just the same way that you would if you didn’t have the proper B vitamins.

Now, you can have too much methionine. Let’s say you ate a steak. Suddenly, you have an influx of methionine into the liver. Just tons of methionine. And it’s not that in net on average through the whole day it would be too much methionine because you need a lot of methyl groups through the whole day that you’re gonna get by recycling homocysteine and methionine all the time. It’s just that in that instant, you suddenly have too much methionine for that moment, and you don’t want to run all your methyltransferases into overdrive because what if you don’t need more creatine? What if you don’t need less dopamine? What if, what if, what if? You need some way to buffer the extra methyl groups."

"And that buffer is glycine. Glycine is an amino acid that is very common throughout the food supply, but it’s far more abundant in collagen-rich proteins, like the type you get in skin and bones when you eat animal products because the collagen molecule has a very unique amino acid composition that’s about a third glycine.

So if you eat chicken breast with the skin and you use the bones to make stock, or if you eat your sardines with the skin and bones in them, you get a lot more glycine. If you eat your skinless, boneless chicken breast and that’s it, or you get the sardines that don’t have the skin and don’t have the bones and that’s it, you’re getting a lot of methionine, and you’re not getting very much glycine.

So you can have this influx of methionine that comes in, and you can be predisposed to at least transient overmethylation in the sense that if you don’t have the glycine buffer to mop up the extra methyl groups, then you have less control over the level of methylation that’s happening in that moment in the postprandial state.

Glycine is going to take up a methyl group and become sarcosine, or it’s gonna take up two methyl groups and become dimethylglycine, and you may pee that out in your urine, or you may salvage it through various pathways where you can eventually get those methyl groups back into the regular system where they could actually recycle homocysteine.

But in general, I think it’s helpful to think of glycine as mainly getting peed out in the urine because if you have some problem of overmethylation, then that’s essentially what it’s gonna do. It’s gonna waste your glycine, and if you don’t have that glycine there, it’s gonna predispose you to rampant overmethylation.

Now, there are also other nutrients because there’s an alternative pathway that operates somewhat less ubiquitously, meaning there are some tissues where it’s not as important as the main pathway we’ve been talking about, but there are certain tissues where it’s very important, and overall, it’s a very important adjunct or alternative to the folate/B12 pathway."

Choline and betaine

"And this is mediated by betaine, or trimethylglycine. You can get betaine from spinach, wheat, or beets, and you can also make your own betaine from choline. And choline is most abundant in liver and egg yolks. You can actually make your own choline too. But when you make your own choline, you have to use methylation to make your own choline.

In fact, every time you make a molecule of phosphatidylcholine—which is how you make choline for the most part, you need to make this choline-containing phospholipid, phosphatidylcholine, and then you can break it apart to get the choline—every time you do that, you have to use three methyl groups and generate three homocysteine molecules. So you can’t get choline from endogenous synthesis to use for methylation. You’re simply taxing your methylation system to make the choline. You could then at a later time use that choline for methylation, but you’re not net gaining anything to support methylation if you’re making your own choline.

So basically to support methylation through this pathway, you want to either get betaine from spinach, wheat, or beets. Betaine is named after beets, but there’s actually more in spinach or wheat. Spinach, notably, does not contain gluten, and so if you’re looking to get a lot of betaine but not much gluten, then spinach is the way to go.

Or you’re getting choline from liver and egg yolks. Liver and egg yolks have far more choline than any other food, but it should be noted that you could piece together a significant choline intake if you eat a lot of foods that have smaller amounts of choline.

As a general principle, there’s smaller amounts of choline in animal foods and in plant foods that are pretty low-carb. So that’s not a universal rule, but if you ate a diversity of low-carb plant foods, lots of vegetables, plenty of nuts, or you ate a lot of meat, all that stuff adds up to a significant amount of choline. It’s just that there’s way more per calorie, per gram food, per any way you measure it in liver and egg yolks. Vastly more.

You can also get choline as a supplement. It comes in many forms. And you can get betaine as a supplement when it is called trimethylglycine. And of course, many people take betaine HCl for stomach acid replacement, and that has some betaine in it as well."

Niacin

"When you take niacin beyond what you need, you methylate it. And it’s becoming very trendy to supplement with nicotinamide riboside for life extension, and that could potentially decimate your methylation pool, at least for a few hours after you take it because the one study that I could find that looked at its methylation showed that the methylated metabolites of niacin hugely spiked in the hours after taking a nicotinamide riboside supplement. So I would look at that as a negative tax on the methylation pool that might not matter if you don’t have any problems here, but if you tend towards not having enough methyl groups, it could make that situation worse."

Creatin

"Creatine is important because 45% of your methylation is actually used for the synthesis of creatine. That means if you eat creatine, you’re gonna take a huge load off of that need for methyl groups.

From what I’ve looked at, you synthesize about a gram and a half of creatine a day, and you can get that from eating about 12 ounces of meat. Now, I think that the people who were measured for the studies that say you make a gram and a half of creatine a day were probably eating 12 ounces of meat, so you’re probably looking at maybe a pound and a half of meat if you wanted to fully replace your need to make creatine. And at that point, you would probably cut your methylation demand in half, at least theoretically.

From supplementation studies, you would think on this basis that a gram and a half of creatine would be sufficient to cut your methylation demand maximally, but there are some studies suggesting that 5 grams of creatine per day is the dose that you might need to really cut your homocysteine down if you have an MTHFR mutation that’s leading to high homocysteine. So I would say I think a gram to—between one and a half and 5 grams of creatine is potentially useful for supporting the methylation system."

"[..]creatine is used even when you’re at rest. You’re always using creatine as a buffer of the ATP supply. You have three to four times more creatine in your muscles than you do ATP, and when the ATP is utilized, it just has three to four times more creatine surrounding it, where the creatine can just donate a phosphate to the ATP and donate energy to recycle the ATP, and that saves ATP from having to make a trip over to the mitochondrion, to go into the mitochondrion, as ADP and phosphate get turned back into ATP, leave the mitochondrion, go back to where it’s needed.

So when we talk about creatine and high-intensity exercise, that’s a context where we would actually see the creatine pool get depleted. If you just look at someone at rest or someone doing easy tasks, you’re not gonna see creatine get depleted, but the creatine is always in flux and always being used. So if your creatine runs low, then your muscles are gonna get tired, even at relatively easy, or what should be easy, tasks."

..

"But what I would say is that if you have vulnerabilities to anxiety or depression or distractibility or hyperactivity or anything that could fit into this model, then there’s two things. Number one is you don’t want to get carried away with this model. This model is a partial tool. There’s absolutely no way that this explains everything about depression and anxiety. These things are physiological and they’re psychological.

So without believing that this is gonna be the key that will let you ignore other factors, like paying attention to how you think or the things that you think about, if you can see in what you’re experiencing a relative excess in mental stability, then animal foods and folate-rich foods that support methylation are likely to make your mental state more fluid.

And that can mean more meat. It could mean more meat for more methionine, or it could mean more meat—methionine you can get from eggs and dairy. Creatine is really about animal flesh. I should say it could mean more animal protein, in general, for methionine, or it could be more meat theoretically up to a pound and a half a day, which, again, you might not want to eat for other reasons, but it could mean that much meat to supply creatine that’s gonna reduce the need for methylation and also supply methionine.

It could mean to eat more liver, legumes, or leafy greens for their folate content. It could mean to eat more liver or egg yolks for their choline content. It could mean to eat more spinach, wheat, or beets for the betaine content. It could mean to supplement with methylfolate. It could mean to supplement with methylcobalamin, a form of vitamin B12. It could mean to supplement with trimethylglycine, another name for betaine. It could mean to supplement with choline. It could mean to stop supplementing with nicotinamide riboside if you’re doing that or high-dose niacin in some other form if that’s sapping your methyl group supply.

On the other hand, if you have the opposite problem of being too distracted, too flighty, and you can’t focus—it’s not that you’re focusing on the wrong things, it’s that you’re not able to focus on anything for very long—then you might need to either look for something that could be contributing to overmethylation. For example, you may be supplementing with too much of whatever I had listed before, or you could be supplementing with SAMe, which I didn’t even list in the last list but which belongs there. SAMe is the principal methyl donor and is pro-methylation, pro-mental fluidity.

If you’re going overboard with those supplements, then that could be putting you into the overmethylation state. Or if you don’t have enough glycine. It could be that whatever your supplements are, your foods are, is demanding more glycine. For example, when you eat more methionine, that demands more glycine. It could be that you have metabolic problems that are way beyond the scope of this podcast that are leading to glycine wasting. Pretty much any block-up in energy metabolism can lead to glycine wasting. MTHFR mutations can lead to glycine wasting, and I’ll talk more about why that’s the case in a later episode about MTHFR.

But if you need more glycine, you could supplement with glycine as a free amino acid, or you could supplement with collagen. If you supplement with collagen, you should beware that it’s theoretically possible, I think the possibility is probably small, but it’s possible that if you have a problem with oxalates, supplementing with collagen could aggravate that. So if you have a vulnerability to kidney stones, for example, you might need to avoid oxalates, and you might want to avoid the collagen. I think that’s not likely to be a huge problem for most people. Collagen is probably ideal as a way to get glycine, and just from experience and talking to people, it seems like it’s better managed digestively than high-dose glycine, but you could try any of those and see what works best for you."​

If some organic salts of potassium have been used to negate acidity from casein (but also chlorid of soda), then organic salts of magnesia must be useful here. Magnesium malate is an example.


Fat is also removed when cheese becomes a major source of proteid. Molybdenum might concentrate in it (paymanz, 2016) (first time that I used 'in' the right way, nice), so it can be lost as well. The consequences of this have been discussed on a previous page.

Contrary to what I thought, replacing whey isn't enough: processing damages nutrients and some might become less available to the body despite not being lost altogether. Since the protein profile is modified, the body will have to adjust it and this demands more nutrition.

Since the aqueous phase of milk provides most of the B-vitamins and these are absorbed earlier, it might be an indicator of how meals should work, preparing the body to process proteids without problems. Otherwise perhaps there could be ways of packing these vitamins in ways that the absorption was slower, such as using fat-soluble forms, I don't know. There must be a good reason why cysteine concentrates in whey as well, and when that is lost (which also happens to some degree when milk is processed (Christopher, 1835)), it might strain the body sooner or later.

As mentioned before, one of them is B6.

Homocysteine in health and disease (ESPN 0-521-65319-3):

"Vitamin B6 is found in many types of foods. Meats (including fish) are excellent sources, as are legumes and bananas; potatoes, whole grain cereal products, and many vegetables are good sources. Fortified breakfast cereals and vitamin supplements are also significant sources (28,51). The major forms of vitamin B6 in foods of animal original (meats, dairy products, et eggs) include pyridoxal 5'-phosphate, pyridoxamine phosphate, pyridoxal, and pyridoxamine. Pyridoxal 5'-phosphate and pyridoxamine phosphate typically are the most abundant in vivo forms of vitamin B6 in animal tissues and products (meats, dairy products, et egges). Glycosylated forms of vitamin B6 do not exist in significant quantities animal tissues and products; however! Foods of plant origin (e.g., fruits, vegetables, grains, legumes) contain from 5% to 75% of their vitamin B6 in glycosylated form. The total concentration and relative proportions of aldehyde (pyridoxal 5'-phosphate and pyridoxal) and amine (pyridoxamine phosphate and pyridoxamine) forms of vitamin B6 differ among tissues. Nonenzymatic transamination reactions that occur during the cooking, storage, or thermal processing of foods [cough] can dramatically alter the ratios of aldehyde and amine forms of the vitamin (33). Pyridoxine notdio-D-glucoside accounts for a high proportion of total vitamin B6 in many common plant-derived foods, with a mean of perhaps one third of total vitamin B6 (34,35,58). Glycosylated vitamin B6 constitutes approximately 15% of the vitamin B6 in many common diets, with a wide range depending on food selection petterns. A typical mixed diet may include all of the various forms of vitamin B6 except pyridoxine phosphate, which is a quantitatively minor intermediate in vitamin B6 metabolism. Differences in in vivo kinetics among pyridoxine, pyridoxal, and pyridoxamine have been reported (113), but all are effectively absorbed and metabolically utilized."​

They comment that in inflammatory conditions ranging from coeliac disease to cirrhosis, cancer, diabetes, renal disease, and other unimportant diseases it's common to find low B6 status. It can be malabsporption, increased utilization, excessive clearance, or impaired conversion to pyridoxal 5'-phosphate, less available depending on the source, etc.

So all these might deserve some consideration. And once again: I suspect that the compensations discussed must work best within the meal.
 

Waremu

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I didn't see Chris say anything about a calcium to magnesium ratio in those quotes. I do however see that he talks a lot about the importance of magnesium in relation to methionine, but not so much why high calcium is bad in relation to methionine. (If so, maybe you can better point it out for me as I may have missed it.)

I think the whole calcium to magnesium ratio topic is a murky area and would like to see more stuff come out that harmonizes the conflicting theories. And I'm not convinced a 1:1 ratio is ideal or natural either, due to some factors I think some don't consider well (for example, human milks calcium to magnesium ratio isn't 1:1, and I don't see how anyone could argue that there is a ratio more natural for humans than our first food, mothers milk). It's extremely hard if not impossible getting a lower end of calcium to magnesium while keeping a decent calcium to phosphorus ratio, in conjunction with the other B vitamins. And in my experience, higher calcium is still much needed to keep PTH very low. From my blood work, I notice that if I am even slightly out of balance with the calcium to phosphorus ratio range, my PTH goes higher and my sleep suffers greatly. Chris Masterjohn mentioned that this is the case for him as well, in his experience. And like Chris, with me, it is a notable immediate effect as well. My bloodwork has shown that my PTH doesn't low enough if my calcium to phosphorous is not at least 1.5:1.

Maybe it's just safer using milk over cheese because you avoid the Vitamin B depletion issues while still getting the whey with the casein which has the cystine, and getting extra magnesium to help balance out the calcium more through fruit, salts, etc.

To me that seems like the safer option than eating a lot of cheese, because it just seems cheese loses many of those important nutrients via processing thus creating larger imbalances than the calcium to magnesium. (It really adds to the overall PUFA as well) And it's actually quite possible to get towards a 3:1 and 2:1 fairly easy with just adding a lot of fruit/greens to some a diet containing fresh milk. You're also getting the choline in the milk. (I consume raw A2 cow/goat milk).

A higher carb diet will already need enough B vitamins, particualry B1. And trying to eat cheese and make up for the already lost B vitamins with the fruit may not be enough because regardless of the cheese, higher carbs require more B1 and other vitamins, so the B vitamins from fruit might merely be making up for the higher carb intake that would be needed regardless of B vitamin depleted foods being add, and then the B depleted foods might possibly create an imbalance that the B vitamins brought to balance out the higher carb intake absent of B depleted foods.

The more I study these things, the more I realize it's probably safer consuming foods in their least processed state due to depletion of nutrients causing nutritional imbalances. Milk and fruit are the freshest foods.

There's a problem in consuming a lot of methionine with way more calcium than magnesium: it can oppose a mineral that's already scarce, which is needed for correct metabolism of methionine (and almost everything else). Of course Chris has some interesting thoughts on it:

- https://www.westonaprice.org/helps-consider-magnesium-metabolic-rate/

"Here, I’d like to chip away at one small piece of the puzzle that I have not written about yet: why benefits from SAMe supplementation should cause one to look not only at the most commonly discussed methylation nutrients (e.g., B12, folate, choline, betaine, methionine) and genetic polymorphisms (e.g., MTHFR) but also at issues that are more commonly neglected when discussing methylation: magnesium and the metabolic rate."

"[..]before methionine can be used for methylation it must be activated to S-adenosyl-methione, which is sold as a supplement and in the supplement market generally abbreviated as SAMe."

"[..]any problems recycling methionine from homocysteine should be fully investigated because if these are the real problems then an expensive supplement like SAMe is a waste of money. These conditions would tend to be associated with elevated levels of homocysteine and they could include deficiencies of B12 or folate, especially in the context of a diet that is not rich in choline or betaine[.]"

"There is another possibility, however, that is strongly suggested by the biochemistry: some people may not be efficiently activating methionine to SAMe. In order for this activation to take place, the enzyme methionine adenosyltransferase (MAT, also known as S-adenosyl methionine synthetase) breaks apart ATP to harvest from it a molecule of adenosine and then activates methionine by sticking adenosine onto it."

"People who have severe genetic deficiencies of the MAT enzyme are unable to use methionine, even when adequately present, for the methylation process. This is because that methionine is never activated to SAMe. Thus, they are deficient in methylation, they have little risk of depleting glycine by consuming excess methionine if the problem isn’t fixed (though they still may have inadequate glycine for other purposes, such as detoxification and synthesizing collagen), and since they never use up the methionine to make homocysteine, their methionine becomes elevated rather than their homocysteine, and their homocysteine is actually low."

"The biochemistry suggests that people with a normally functioning MAT gene could have two other reasons for poor activation of methionine: poor magnesium status, or a low metabolic rate. Since ATP is the source of the activating molecule, the reaction is, quite clearly, ATP-dependent. Since ATP is always utilized as a chelate with magnesium, the reaction is also magnesium-dependent. The presence of a magnesium deficiency, a low metabolic rate, or both conditions together, could prevent methionine from being activated."

"It is important to realize, however, that a low metabolic rate or a magnesium deficiency will compromise thousands of bodily processes, and that either condition would be likely to coexist with multiple nutrient deficiencies. Thus, such a person will not necessarily replicate the presentation of someone with a genetic deficiency of the MAT enzyme. They will not, for example, necessarily have low homocysteine. If the recycling of homocysteine is also being compromised, then homocysteine could be normal or elevated even while methionine is failing to be utilized properly and is thereby generating homocysteine at a much lower rate."

"In my opinion, if someone benefits from SAMe supplementation or suffers from any of the conditions for which SAMe supplementation has shown to be beneficial, and it can be ruled out that simply ensuring adequacy of dietary methionine and relevant B vitamins would fix the problem, magnesium status and metabolic rate should be evaluated."

"Ensuring a normal basal body temperature is, in my current opinion, probably the most cost-effective and helpful way to address the metabolic rate. However, addressing why the metabolism may have slowed may be more complicated."​

- https://chrismasterjohnphd.com/2017/07/17/methylate-way-mental-health-dopamine/

"So first of all, the principal methyl donor for hundreds of different methylation reactions is S-adenosylmethionine. You take methionine, which is an amino acid that comes from your dietary protein and which is found in animal proteins and plant proteins but which is twice as abundant in animal proteins as it is in plant proteins—you take methionine, and then you activate it using magnesium and ATP. ATP is adenosine triphosphate. If you break apart the phosphates at the end, you get energy. But if you break all of them off, you get adenosine. And if you take that adenosine and you take that energy and you tack it onto the methionine molecule, you get S-adenosylmethionine. That requires ATP. Everything that requires ATP requires magnesium because ATP does everything it does as a chelate of magnesium."

"So once you have methionine in from your dietary protein and you activate it using magnesium and ATP, you have S-adenosylmethionine. Now, this—which is incidentally sold as a supplement as often colloquially called SAMe—this is the principal methyl donor that through hundreds of different reactions mediated by different enzymes that are all called some variation of a methyltransferase, you take this methyl group from S-adenosylmethionine, and you donate it to something else."

"If you have methionine, and you take away a methyl group—which incidentally is where methionine gets its name from: “meth-” from methyl group and “-thi-” coming from the Greek theîon, meaning sulfur, and this is because if you look at the methionine molecule, you would see that it’s one of the two amino acids that contains sulfur in it. The other one is cysteine, so it’s one of the two sulfur amino acids. And on the end of that sulfur, that sulfur is capped by a methyl group, and that’s the methyl group that you remove when you methylate things, like dopamine or precursors to creatine."

"Once you get rid of that methyl group, you would have homocysteine. But because you’re using S-adenosylmethionine, what you actually have left over is S-adenosylhomocysteine. You then hydrolyze the adenosyl group from that, meaning the adenosine from ATP that you stuck onto it, you now take off. With that, you can regenerate ATP in the system of energy metabolism."

"But now you have homocysteine, and homocysteine is normal to have, it’s important to have, it’s always a byproduct of this system. But many of you may know homocysteine as something that goes high when you have higher heart disease risk. So homocysteine is often measured in the blood for that reason. If your homocysteine is high, it’s taken as an indication that you have greater risk of heart disease, and that’s because homocysteine can cause oxidative stress and can damage blood vessels. But if we’re paying attention to how the system works, high homocysteine is probably more problematic simply as a result of this system being defective."

"So what do you do with that homocysteine? Well, there’s two principal fates of homocysteine. One is that if you have a lot of it, more than you need for methylation, you can turn it into cysteine using the help of vitamin B6 and of the amino acids serine or glycine. And with that cysteine, you can turn it into taurine or sulfate or glutathione.

Taurine is important for the electrical activity in the brain and retina. Sulfate is important for many things in regulating hormones and promoting detoxification and other uses. Glutathione is an antioxidant, in fact the central antioxidant of the cell, but also important in detoxification, it regulates hundreds of proteins, protects the lungs from oxidative stress, makes mucus fluid, does all kinds of great things like that. So if you have lots and lots and lots of homocysteine, you might be putting it into cysteine so it can go down through those pathways.

But the first thing you do with homocysteine, the regular thing you do with homocysteine, the thing that you’re pretty much always doing with homocysteine in between your meals when you didn’t just eat a huge methionine load from a steak, is you are recycling the homocysteine back to methionine.

Now, imagine that you ate this methionine from your steak or wherever it came from, you only used it once, and that methyl group is gone, so maybe you synthesized one molecule of creatine or part of a molecule of creatine, or you got rid of one molecule of dopamine. Whatever you did with that methyl group, the methyl group is now permanently gone.

So most of your methylation is actually coming from being able to recycle the homocysteine. How do you recycle it? Well, you have folate, which takes a methyl group from breaking down other amino acids and transferring it to vitamin B12. Vitamin B12 then transfers it to homocysteine. That sticks the methyl group back on the end of the molecule to cap that sulfur to get methionine, the methyl-capped sulfur amino acid. And once you do that, you can then activate it again using ATP and magnesium, and you get S-adenosylmethionine, and you can do another methylation cycle. Then you get homocysteine again, you gotta just do it over and over and over again.

Now, every time you recycle it, you are not consuming folate or B12. You’re simply consuming methyl groups that they are transferring. So you don’t need a molecule of folate to support one turn of the methylation cycle, but you need enough folate that you can keep the delivery of methyl groups going. You need enough B12 that you can keep the delivery of the methyl groups going. So if you don’t have incoming methyl groups from your amino acid metabolism, you can’t keep this system going. If you don’t have enough folate, you can’t keep it going. If you don’t have enough B12, you can’t keep it going.

Now, the system whereby folate gets its methyl group is actually really complicated, and I’m not gonna go into all the details, but I’ll say that your energy metabolism has to be working properly. You’re gonna have to have enough niacin, which is vitamin B3. You’re gonna have to have enough riboflavin, which is vitamin B2. You’re gonna have to have enough thiamin, which is vitamin B1. There’s various genetics that lie outside the methylation pathway that could impact this.

And of course, there’s famous genetics inside the methylation pathway that affect this. For example, MTHFR, that gene that really stands for 5,10-methylenetetrahydrofolate reductase, but you know what it looks like it means. I’m not marking this episode explicit, so I’m gonna skip that. You know what I’m talking about.

Anyway, the MTHFR gene is coding for the enzyme that does the final construction of the methyl group on folate. So if you have low MTHFR activity, then you are not gonna be able to get the methyl groups going through to homocysteine in just the same way that you would if you didn’t have the proper B vitamins.

Now, you can have too much methionine. Let’s say you ate a steak. Suddenly, you have an influx of methionine into the liver. Just tons of methionine. And it’s not that in net on average through the whole day it would be too much methionine because you need a lot of methyl groups through the whole day that you’re gonna get by recycling homocysteine and methionine all the time. It’s just that in that instant, you suddenly have too much methionine for that moment, and you don’t want to run all your methyltransferases into overdrive because what if you don’t need more creatine? What if you don’t need less dopamine? What if, what if, what if? You need some way to buffer the extra methyl groups."

"And that buffer is glycine. Glycine is an amino acid that is very common throughout the food supply, but it’s far more abundant in collagen-rich proteins, like the type you get in skin and bones when you eat animal products because the collagen molecule has a very unique amino acid composition that’s about a third glycine.

So if you eat chicken breast with the skin and you use the bones to make stock, or if you eat your sardines with the skin and bones in them, you get a lot more glycine. If you eat your skinless, boneless chicken breast and that’s it, or you get the sardines that don’t have the skin and don’t have the bones and that’s it, you’re getting a lot of methionine, and you’re not getting very much glycine.

So you can have this influx of methionine that comes in, and you can be predisposed to at least transient overmethylation in the sense that if you don’t have the glycine buffer to mop up the extra methyl groups, then you have less control over the level of methylation that’s happening in that moment in the postprandial state.

Glycine is going to take up a methyl group and become sarcosine, or it’s gonna take up two methyl groups and become dimethylglycine, and you may pee that out in your urine, or you may salvage it through various pathways where you can eventually get those methyl groups back into the regular system where they could actually recycle homocysteine.

But in general, I think it’s helpful to think of glycine as mainly getting peed out in the urine because if you have some problem of overmethylation, then that’s essentially what it’s gonna do. It’s gonna waste your glycine, and if you don’t have that glycine there, it’s gonna predispose you to rampant overmethylation.

Now, there are also other nutrients because there’s an alternative pathway that operates somewhat less ubiquitously, meaning there are some tissues where it’s not as important as the main pathway we’ve been talking about, but there are certain tissues where it’s very important, and overall, it’s a very important adjunct or alternative to the folate/B12 pathway."

Choline and betaine

"And this is mediated by betaine, or trimethylglycine. You can get betaine from spinach, wheat, or beets, and you can also make your own betaine from choline. And choline is most abundant in liver and egg yolks. You can actually make your own choline too. But when you make your own choline, you have to use methylation to make your own choline.

In fact, every time you make a molecule of phosphatidylcholine—which is how you make choline for the most part, you need to make this choline-containing phospholipid, phosphatidylcholine, and then you can break it apart to get the choline—every time you do that, you have to use three methyl groups and generate three homocysteine molecules. So you can’t get choline from endogenous synthesis to use for methylation. You’re simply taxing your methylation system to make the choline. You could then at a later time use that choline for methylation, but you’re not net gaining anything to support methylation if you’re making your own choline.

So basically to support methylation through this pathway, you want to either get betaine from spinach, wheat, or beets. Betaine is named after beets, but there’s actually more in spinach or wheat. Spinach, notably, does not contain gluten, and so if you’re looking to get a lot of betaine but not much gluten, then spinach is the way to go.

Or you’re getting choline from liver and egg yolks. Liver and egg yolks have far more choline than any other food, but it should be noted that you could piece together a significant choline intake if you eat a lot of foods that have smaller amounts of choline.

As a general principle, there’s smaller amounts of choline in animal foods and in plant foods that are pretty low-carb. So that’s not a universal rule, but if you ate a diversity of low-carb plant foods, lots of vegetables, plenty of nuts, or you ate a lot of meat, all that stuff adds up to a significant amount of choline. It’s just that there’s way more per calorie, per gram food, per any way you measure it in liver and egg yolks. Vastly more.

You can also get choline as a supplement. It comes in many forms. And you can get betaine as a supplement when it is called trimethylglycine. And of course, many people take betaine HCl for stomach acid replacement, and that has some betaine in it as well."

Niacin

"When you take niacin beyond what you need, you methylate it. And it’s becoming very trendy to supplement with nicotinamide riboside for life extension, and that could potentially decimate your methylation pool, at least for a few hours after you take it because the one study that I could find that looked at its methylation showed that the methylated metabolites of niacin hugely spiked in the hours after taking a nicotinamide riboside supplement. So I would look at that as a negative tax on the methylation pool that might not matter if you don’t have any problems here, but if you tend towards not having enough methyl groups, it could make that situation worse."

Creatin

"Creatine is important because 45% of your methylation is actually used for the synthesis of creatine. That means if you eat creatine, you’re gonna take a huge load off of that need for methyl groups.

From what I’ve looked at, you synthesize about a gram and a half of creatine a day, and you can get that from eating about 12 ounces of meat. Now, I think that the people who were measured for the studies that say you make a gram and a half of creatine a day were probably eating 12 ounces of meat, so you’re probably looking at maybe a pound and a half of meat if you wanted to fully replace your need to make creatine. And at that point, you would probably cut your methylation demand in half, at least theoretically.

From supplementation studies, you would think on this basis that a gram and a half of creatine would be sufficient to cut your methylation demand maximally, but there are some studies suggesting that 5 grams of creatine per day is the dose that you might need to really cut your homocysteine down if you have an MTHFR mutation that’s leading to high homocysteine. So I would say I think a gram to—between one and a half and 5 grams of creatine is potentially useful for supporting the methylation system."

"[..]creatine is used even when you’re at rest. You’re always using creatine as a buffer of the ATP supply. You have three to four times more creatine in your muscles than you do ATP, and when the ATP is utilized, it just has three to four times more creatine surrounding it, where the creatine can just donate a phosphate to the ATP and donate energy to recycle the ATP, and that saves ATP from having to make a trip over to the mitochondrion, to go into the mitochondrion, as ADP and phosphate get turned back into ATP, leave the mitochondrion, go back to where it’s needed.

So when we talk about creatine and high-intensity exercise, that’s a context where we would actually see the creatine pool get depleted. If you just look at someone at rest or someone doing easy tasks, you’re not gonna see creatine get depleted, but the creatine is always in flux and always being used. So if your creatine runs low, then your muscles are gonna get tired, even at relatively easy, or what should be easy, tasks."

..

"But what I would say is that if you have vulnerabilities to anxiety or depression or distractibility or hyperactivity or anything that could fit into this model, then there’s two things. Number one is you don’t want to get carried away with this model. This model is a partial tool. There’s absolutely no way that this explains everything about depression and anxiety. These things are physiological and they’re psychological.

So without believing that this is gonna be the key that will let you ignore other factors, like paying attention to how you think or the things that you think about, if you can see in what you’re experiencing a relative excess in mental stability, then animal foods and folate-rich foods that support methylation are likely to make your mental state more fluid.

And that can mean more meat. It could mean more meat for more methionine, or it could mean more meat—methionine you can get from eggs and dairy. Creatine is really about animal flesh. I should say it could mean more animal protein, in general, for methionine, or it could be more meat theoretically up to a pound and a half a day, which, again, you might not want to eat for other reasons, but it could mean that much meat to supply creatine that’s gonna reduce the need for methylation and also supply methionine.

It could mean to eat more liver, legumes, or leafy greens for their folate content. It could mean to eat more liver or egg yolks for their choline content. It could mean to eat more spinach, wheat, or beets for the betaine content. It could mean to supplement with methylfolate. It could mean to supplement with methylcobalamin, a form of vitamin B12. It could mean to supplement with trimethylglycine, another name for betaine. It could mean to supplement with choline. It could mean to stop supplementing with nicotinamide riboside if you’re doing that or high-dose niacin in some other form if that’s sapping your methyl group supply.

On the other hand, if you have the opposite problem of being too distracted, too flighty, and you can’t focus—it’s not that you’re focusing on the wrong things, it’s that you’re not able to focus on anything for very long—then you might need to either look for something that could be contributing to overmethylation. For example, you may be supplementing with too much of whatever I had listed before, or you could be supplementing with SAMe, which I didn’t even list in the last list but which belongs there. SAMe is the principal methyl donor and is pro-methylation, pro-mental fluidity.

If you’re going overboard with those supplements, then that could be putting you into the overmethylation state. Or if you don’t have enough glycine. It could be that whatever your supplements are, your foods are, is demanding more glycine. For example, when you eat more methionine, that demands more glycine. It could be that you have metabolic problems that are way beyond the scope of this podcast that are leading to glycine wasting. Pretty much any block-up in energy metabolism can lead to glycine wasting. MTHFR mutations can lead to glycine wasting, and I’ll talk more about why that’s the case in a later episode about MTHFR.

But if you need more glycine, you could supplement with glycine as a free amino acid, or you could supplement with collagen. If you supplement with collagen, you should beware that it’s theoretically possible, I think the possibility is probably small, but it’s possible that if you have a problem with oxalates, supplementing with collagen could aggravate that. So if you have a vulnerability to kidney stones, for example, you might need to avoid oxalates, and you might want to avoid the collagen. I think that’s not likely to be a huge problem for most people. Collagen is probably ideal as a way to get glycine, and just from experience and talking to people, it seems like it’s better managed digestively than high-dose glycine, but you could try any of those and see what works best for you."​

If some organic salts of potassium have been used to negate acidity from casein (but also chlorid of soda), then organic salts of magnesia must be useful here. Magnesium malate is an example.


Fat is also removed when cheese becomes a major source of proteid. Molybdenum might concentrate in it (paymanz, 2016) (first time that I used 'in' the right way, nice), so it can be lost as well. The consequences of this have been discussed on a previous page.

Contrary to what I thought, replacing whey isn't enough: processing damages nutrients and some might become less available to the body despite not being lost altogether. Since the protein profile is modified, the body will have to adjust it and this demands more nutrition.

Since the aqueous phase of milk provides most of the B-vitamins and these are absorbed earlier, it might be an indicator of how meals should work, preparing the body to process proteids without problems. Otherwise perhaps there could be ways of packing these vitamins in ways that the absorption was slower, such as using fat-soluble forms, I don't know. There must be a good reason why cysteine concentrates in whey as well, and when that is lost (which also happens to some degree when milk is processed (Christopher, 1835)), it might strain the body sooner or later.

As mentioned before, one of them is B6.

Homocysteine in health and disease (ESPN 0-521-65319-3):

"Vitamin B6 is found in many types of foods. Meats (including fish) are excellent sources, as are legumes and bananas; potatoes, whole grain cereal products, and many vegetables are good sources. Fortified breakfast cereals and vitamin supplements are also significant sources (28,51). The major forms of vitamin B6 in foods of animal original (meats, dairy products, et eggs) include pyridoxal 5'-phosphate, pyridoxamine phosphate, pyridoxal, and pyridoxamine. Pyridoxal 5'-phosphate and pyridoxamine phosphate typically are the most abundant in vivo forms of vitamin B6 in animal tissues and products (meats, dairy products, et egges). Glycosylated forms of vitamin B6 do not exist in significant quantities animal tissues and products; however! Foods of plant origin (e.g., fruits, vegetables, grains, legumes) contain from 5% to 75% of their vitamin B6 in glycosylated form. The total concentration and relative proportions of aldehyde (pyridoxal 5'-phosphate and pyridoxal) and amine (pyridoxamine phosphate and pyridoxamine) forms of vitamin B6 differ among tissues. Nonenzymatic transamination reactions that occur during the cooking, storage, or thermal processing of foods [cough] can dramatically alter the ratios of aldehyde and amine forms of the vitamin (33). Pyridoxine notdio-D-glucoside accounts for a high proportion of total vitamin B6 in many common plant-derived foods, with a mean of perhaps one third of total vitamin B6 (34,35,58). Glycosylated vitamin B6 constitutes approximately 15% of the vitamin B6 in many common diets, with a wide range depending on food selection petterns. A typical mixed diet may include all of the various forms of vitamin B6 except pyridoxine phosphate, which is a quantitatively minor intermediate in vitamin B6 metabolism. Differences in in vivo kinetics among pyridoxine, pyridoxal, and pyridoxamine have been reported (113), but all are effectively absorbed and metabolically utilized."​

They comment that in inflammatory conditions ranging from coeliac disease to cirrhosis, cancer, diabetes, renal disease, and other unimportant diseases it's common to find low B6 status. It can be malabsporption, increased utilization, excessive clearance, or impaired conversion to pyridoxal 5'-phosphate, less available depending on the source, etc.

So all these might deserve some consideration. And once again: I suspect that the compensations discussed must work best within the meal.
 
Last edited:

Ella

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What exactly do you mean by this? With regard to palatability? Enhanced absorption of iron from vitamin C? Cooked apples go quite well with liver IMO, along with coffee to inhibit iron absorption, gelatin to balance out the unfavorable amino acid profile, and milk (calcium) to balance the phosphate in liver.
@loess love apples with liver. I normally serve liver pate with a fruit platter.

Fruit also helps to balance the high phosphate in liver. There is the risk of increasing iron absorption which as you highlighted; easily mitigated with coffee and milk.

Peat (some where??) mentions the ratio of phosphate to calcium can go as high as 4 to 1 if there is plenty of fruit and sugar in the diet.

My phosphate went too low by reducing high phosphate foods, like grains, breads, pasta and consuming high fruit diet, milk and sugar diet. I not saying this was necessarily bad because my phosphate was too high and the reason I suffered kidney stress >10 years ago which has resolved. I may have been over zealous with the fruit. At the time, I was completely clueless about the phosphate issue and was only focused on improving thyroid function and weight loss.
 
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Amazoniac

Amazoniac

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I didn't see Chris say anything about a calcium to magnesium ratio in those quotes. I do however see that he talks a lot about the importance of magnesium in relation to methionine, but not so much why high calcium is bad in relation to methionine. (If so, maybe you can better point it out for me as I may have missed it.)

I think the whole calcium to magnesium ratio topic is a murky area and would like to see more stuff come out that harmonizes the conflicting theories. And I'm not convinced a 1:1 ratio is ideal or natural either, due to some factors I think some don't consider well (for example, human milks calcium to magnesium ratio isn't 1:1, and I don't see how anyone could argue that there is a ratio more natural for humans than our first food, mothers milk). It's extremely hard if not impossible getting a lower end of calcium to magnesium while keeping a decent calcium to phosphorus ratio, in conjunction with the other B vitamins. And in my experience, higher calcium is still much needed to keep PTH very low. From my blood work, I notice that if I am even slightly out of balance with the calcium to phosphorus ratio range, my PTH goes higher and my sleep suffers greatly. Chris Masterjohn mentioned that this is the case for him as well, in his experience. And like Chris, with me, it is a notable immediate effect as well. My bloodwork has shown that my PTH doesn't low enough if my calcium to phosphorous is not at least 1.5:1.

Maybe it's just safer using milk over cheese because you avoid the Vitamin B depletion issues while still getting the whey with the casein which has the cystine, and getting extra magnesium to help balance out the calcium more through fruit, salts, etc.

To me that seems like the safer option than eating a lot of cheese, because it just seems cheese loses many of those important nutrients via processing thus creating larger imbalances than the calcium to magnesium. (It really adds to the overall PUFA as well) And it's actually quite possible to get towards a 3:1 and 2:1 fairly easy with just adding a lot of fruit/greens to some a diet containing fresh milk. You're also getting the choline in the milk. (I consume raw A2 cow/goat milk).

A higher carb diet will already need enough B vitamins, particualry B1. And trying to eat cheese and make up for the already lost B vitamins with the fruit may not be enough because regardless of the cheese, higher carbs require more B1 and other vitamins, so the B vitamins from fruit might merely be making up for the higher carb intake that would be needed regardless of B vitamin depleted foods being add, and then the B depleted foods might possibly create an imbalance that the B vitamins brought to balance out the higher carb intake absent of B depleted foods.

The more I study these things, the more I realize it's probably safer consuming foods in their least processed state due to depletion of nutrients causing nutritional imbalances. Milk and fruit are the freshest foods.
Milk is meant for a baby with brutal metabolism that makes good use of magnesium. Since absorption and retention tends to be poor when it slows down, extra magnesium within the meal should be helpful. If taken away from the meal, by the time you ingest the cheese, the only thing that's left from magnesium might be its trail.

Thank you for posting the calcium content of fruits else and where.
the new high light color works.....
I changed it after your threat but it's not as ridiculous.
 
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Amazoniac

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@Wagner83 made a good observation here about cheese made from whey perhaps being a good source. So..

- Determination of Vitamin B12 in Dairy Products by Ultra Performance Liquid Chromatography-Tandem Mass Spectrometry

"Results showed a level of vitamin B12 about 10 times higher in whey and ricotta cheese with respect to the milk they are derived from; at the same time, it is interesting to notice a decrease of cobalamine concentration in curd, caciotta cheese and mozzarella cheese (Figure 1). Vitamin B12 affinity for proteins is well known and several kinds of carrier proteins, called transcobalamines, have been identified; these molecules bind cobalamin to protect it from degradation and some analogues are present in bovine milk as well (Fedosov et al., 1995, 1996; Fox and Kelly, 2003; Le et al., 2011)."

upload_2018-8-18_14-55-3.png
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"These data would confirm the tendency of cobalamine to concentrate in the proteic fraction of whey along the cheese production process. The lower value for mozzarella cheese compared to curd is probably due to the process of production, which implies curd draining and a dilution effect related to the water addition in the stretching phase."​
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However! Those values are unusual compared to the majority that I've found so far.

As suspected elsewhere, B12 is indeed unstable in light. If milch is meant to pass directly from the mother to the babyzord, there's no point in protecting it from light; contrary to meats that can't allow it to degraded.

- Vitamin B12 determination in milk, whey and different by-products of ricotta cheese production by ultra performance liquid chromatography coupled with tandem mass spectrometry

"[Cobalamin] shows stability to pH variations between 4 to 7 and to heating up to 120°C, while is highly unstable when exposed to light (Watanabe et al., 2013; Eitenmiller et al., 2008)."

"The average vitamin B12 amount determined in ricotta was [0.0057 mcg]/g in June, [0.02 mcg]/g in November and [0.0049 mcg]/g in February dairy experiment."

upload_2018-8-18_15-7-38.png

Package A: photoprotected
Package B: transparent
Light: left under illuminated conditions
No light: left in the darkness [this must be a song]

(This experiment was quite confusing in general. Part due to language barrier, but other part was just unnecessary complication.)
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"Ricotta cheese samples wrapped in photoprotected packaging seem to be better preserved and B12 levels appear to remain stable up to 48 hours; between the 2nd and 3rd day vitamin B12 content undergo a rapid decrease. Finally, at 96 hours all samples converge to the same low concentration range."​
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For those that prepare your own cheeses, it might be helpful to keep them in a ceramic pot or some opaque container and prepare smaller amounts at a time.

- Light, Riboflavin Degradation And Their Interaction In Milk
- Dairy - Package Protection And Preservation
 
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Amazoniac

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One container of defatted yogurt provides about 17 grams of proteid. Every food here was matched for that same amount, not serving! Later I doubled it just because it's easier to work with larger numbers. So, everything here is based on what you get when 34 grams of protein of a given food are eaten.

It ended up being more or less the following:
  • 2 containers - Generic greek yogurt
  • 2 containers - Fage
  • 340 g - Cottage cheese
  • 200 g - Pot cheese
  • 150 g - Atlantic cod
  • 110 g - Chicken breast
  • 120 g - Beef steak
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upload_2018-9-11_9-1-9.png


upload_2018-9-11_9-1-16.png


upload_2018-9-11_9-2-30.png


upload_2018-9-11_9-2-38.png
upload_2018-9-11_9-2-47.png
upload_2018-9-11_9-2-53.png

To get more accurate values I multiplied the servings by 10 in Cron-o-meter, copied, then divided by 10 just to avoid automatic rounding.
 
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Wagner83

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One container of defatted yogurt provides about 17 grams of proteid. Every food here was matched for that same amount, not serving! Later I doubled it just because it's easier to work with larger numbers. So, everything here is based on what you get when 34 grams of protein of a given food are eaten.

It ended up being more or less the following:
  • 2 containers - Generic greek yogurt
  • 2 containers - Fage
  • 340 g - Cottage cheese
  • 200 g - Pot cheese
  • 150 g - Atlantic cod
  • 110 g - Chicken breast
  • 120 g - Beef steak

To get more accurate values I multiplied the servings by 10 in Cron-o-meter, copied, then divided by 10 just to avoid automatic rounding.
Thanks a ton, where do I donate? Fage and greek yogurt look pretty great and much better than cottage cheese (without considering lactic acid etc..).
 
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Amazoniac

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Thanks a ton, where do I donate? Fage and greek yogurt look pretty great and much better than cottage cheese (without considering lactic acid etc..).
I was wondering if it's possible that the B12 in yogurts has been consumed by bacteria, rendering it less useful despite showing high content.
 

dreamcatcher

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So for vegans is it mandatory to take a b12 supplement? I know there are some who say they didn't need one.

Herbivores don’t produce vitamin B12. All animals require B12, but no animal produces it. The only organisms that produce B12 are bacteria, and so every animal must somehow obtain it either from bacteria or by eating other animals. Different herbivores cope with this in different ways.

Ruminants (sheep, cattle, deer, etc.) have extra chambers in front of their stomachs called the rumen and reticulum that harbor many kinds of bacteria. These bacteria break down the plant material eaten by the ruminant, and also produce B12 and other vitamins. The mass of fermented plant material, bacteria, and vitamins then passes through the animal’s stomach where it is digested, and then to the intestine where the nutrients are absorbed just as they are in humans.

Other herbivores do not have these pre-stomach chambers, but many also have an extra chamber in their intestines called the cecum. This sits between the small and large intestines, and also harbors a large population of bacteria. These bacteria help to finish digesting the plant material and also make B12, which is then absorbed through the wall of the cecum.

Rabbits, on the other hand, run their food through the digestive system twice. The first time, they poop partially-digested food, and then eat these “pellets” so that they can digest them some more. They have bacteria in their colons which produce B12, which they can then absorb when the food passes through their intestines the second time around.

Pandas have none of these mechanisms, and so must eat some animals (mostly insects) along with their primary diet of bamboo. They simply have no other way of getting B12. Most people think of pandas as completely herbivorous, but that is not true.

Humans and the other great apes must also eat some animals in order to get B12. Most people think of gorillas as herbivores, but like the pandas they are not. They consume numerous insects that cling to the leaves that form the bulk of their diet, and this is enough to meet their requirement for B12. Chimpanzees and bonobos (our closest relatives) will actually hunt and eat meat on occasion in addition to consuming insects. Humans and the other great apes all harbor bacteria in our colons that make B12, but unfortunately we are not able to absorb it efficiently through the walls of the colon and so we cannot get our requirement that way. Except for people living in modern societies that can manufacture vitamin supplements, humans must eat some animal food or die.

As to why we didn’t evolve any other mechanism for getting B12, I think the best explanation is that it is easy for us and the other great apes to get what we need by eating small amounts of meat, and so there was no evolutionary pressure toward any of these other anatomical features. In fact, the ancestors of primates used to have a cecum which in modern primates is now atrophied. So apparently, it did not have sufficient survival value to be retained. In humans, the only remnant is the vermiform appendix.

Source: quora
 

tara

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In fact, the ancestors of primates used to have a cecum which in modern primates is now atrophied. So apparently, it did not have sufficient survival value to be retained. In humans, the only remnant is the vermiform appendix.
IIUC, we do still have a cecum. It's between the small and large intestine, it's where the appendix attaches, but it's not the same thing as the appendix.
 
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Amazoniac

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One container of defatted yogurt provides about 17 grams of proteid. Every food here was matched for that same amount, not serving! Later I doubled it just because it's easier to work with larger numbers. So, everything here is based on what you get when 34 grams of protein of a given food are eaten.

It ended up being more or less the following:
  • 2 containers - Generic greek yogurt
  • 2 containers - Fage
  • 340 g - Cottage cheese
  • 200 g - Pot cheese
  • 150 g - Atlantic cod
  • 110 g - Chicken breast
  • 120 g - Beef steak

To get more accurate values I multiplied the servings by 10 in Cron-o-meter, copied, then divided by 10 just to avoid automatic rounding.
Regarding these values, cheese and yogurt don't provide nowhere near as much niacin and choline as meats. A bit less pyridoxine as well. Creatine is another component that's lacking. Also, less carnitine, but may not be as relevant as the others.
 

Reaper242xx

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I eat a fair amount of cheese, though I would consider it my main protein source. Milk, bone broth, gelatin, potatoes, leafy greens, oysters, liver, are my main sources. Cheese is good for a snack or something, when it's paired with fruits. The best thing about cheese is it gives you an extra supplemental dose of calcium whenever you eat it.
 

dreamcatcher

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I eat a fair amount of cheese, though I would consider it my main protein source. Milk, bone broth, gelatin, potatoes, leafy greens, oysters, liver, are my main sources. Cheese is good for a snack or something, when it's paired with fruits. The best thing about cheese is it gives you an extra supplemental dose of calcium whenever you eat it.
+1 and it's good to have variety of foods!!
 

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