The Travis Corner

[ecstatichamster]

Correct me if I'm wrong but I believe that Threonate is Threonic Acid (Metabolite of Ascorbic Acid)...So not the same as Threonine.

threonate is a salt of l-threonine amino, so it should be fine with magnesium...maybe I'm wrong...

 

[Travis]

threonate is a salt of l-threonine amino, so it should be fine with magnesium...maybe I'm wrong...

A person would certainly think so, I would think so, and even some Doctorates of Chemistry would probably think so but this is not the case: The amino acid threonine certainly has a carboxylic acid group (where the 'acid' part comes in) and when this is then deprotonated you'd think it'd then receive an '-ate' suffix like most any carboxylic acid does. This actually does happen, but the carboxylic acid base of threonine has an additional '-in-' interposed within the name: This is given the name threoninate, and not threonate because that had already been taken:

'Threonine was the last of the 20 common proteinogenic amino acids to be discovered. It was discovered in 1936 by William Cumming Rose, collaborating with Curtis Meyer. The amino acid was named threonine because it was similar in structure to threonic acid, a four-carbon monosaccharide with molecular formula C₄H₈O₅.' —Wikipedia​

The name of the amino acid threonine itself derives from threonic acid, which differs only in two respects: (1) the hydroxyl group of the α-carbon is replaced by an amino group; and (2) the hydroxyl group at the C-4 carbon is absent. The stereochemistry is the same in both cases: Just like the amino acid threonine, the L-enantiomer of threonic acid is also the one more commonly found in nature.

So magnesium threoninate would be the one to buy, but this is not commonly available. I still think L-threonine is one of the safest amino acids and its similarity to a vitamin C metabolite only accentuates this fact. Furthermore, excessive amounts will become methylglyoxal in the body through an aminoacetone intermediate. This is effective against cancer, somehow, and there are a few logical mechanisms proposed to account for this; however, my own explanation involves polyamines and nitric oxide: What is peculiar to methylgyloxal and methylglyoxal alone is its ability to form a cyclic conjugate with arginine, like so:

​

This of course nullifies arginine, an amino acid necessary for both polyamine (via ornithine) and nitric oxide synthesis. The former can be found in the cell nucleus directly binding with DNA; it catalyzes transcription by inducing the radical Z-DNA conformation—having a left-handed helix—and an additional spermine always increases the rate of replication during PCR. The latter (ṄO) combines with superoxide in the body to form peroxynitrite (ONOO⁻), which is actually the second sub-
strate for cyclooxygenase besides arachidonic acid (20∶4). The peroxynitrite adds to arachidonic acid to form prostaglandin H₂—the precursor form prostaglandin E₂. The endoperoxide bridge characteristic of prostaglandin H₂ had actually formerly been the peroxide group of peroxynitrite (ONOO⁻ ⟶ ṄO + O–O⁻). This means that arginine is unique in being an obligate precursor for the biosynthesis of the two most potent (endogenous) carcinogens known: the polyamine spermine and prostaglandin E₂. Of course arginine needs help from methionine and linoleic acid to form these compounds, but the carcinogenic effects of those can help infer what you could anticipate from either ingesting or inhibiting the other precursor: arginine.

Methylglyoxal could be expected to abrogate both polyamine and nitric oxide synthesis by irreversibly transforming arginine into hydroimidazalone.​

 

[Amazoniac]

The one and only Nobel aureolate.

 

[ecstatichamster]

thank you @Travis

Do you think that methionine can be blocked when someone is consuming muscle meat, through consumption of collagen or bone broth? Are there strategies for blocking methionine that you have researched or come up with? Dr. Peat and many others now believe, as you indicated, that the life extending benefits of fasting are likely due to low methionine (Peat also believes it is because of lower endotoxins.)

Edited to add: "cheeses" such as ricotta has a lot of l-threonine. Whey cheeses in other words...

 

[Travis]

So magnesium threoninate

thank you @Travis

Do you think that methionine can be blocked when someone is consuming muscle meat, through consumption of collagen or bone broth? Are there strategies for blocking methionine that you have researched or come up with? Dr. Peat and many others now believe, as you indicated, that the life extending benefits of fasting are likely due to low methionine (Peat also believes it is because of lower endotoxins.)

Edited to add: "cheeses" such as ricotta has a lot of l-threonine. Whey cheeses in other words...

Yeah. I think the best natural inhibitor is selenomethionine, which has been shown to lower colon cancer in rats. You can find a handful of articles on this, but most just deal with selenium-enriched broccoli. [All Brassica species are selenium hyperaccumulators and will store it as selenomethionine.] The cancer reductions seen in broccoli experiments are notable, and these are still sometimes often (wrongly) explained through broccoli cyanogenic glycosides. However, experiments using soil selenium-enriched broccoli vs. control broccoli indicate that it's the selenomethionine which is causing the cancer reductions. Also, there was a prospective study done using selenium supplementation (from Se-enriched yeast) on prostate cancer incidence showing something like a 63% reduction.⁽¹⁾ But one has to be a bit discerning in this area, since some studies just use inorganic selenide and many researchers still assume a false equivalency between the two. Notions of the selenium ion alone—or selenate—being responsible for these effects must at once be discarded with prejudice; I think anyone who investigates this will conclude that selenomethionine inhibits cancer proliferation by inhibiting polyamine synthetic enzymes, and also that inorganic selenide works only to the extent that it's used for de novo selenomethionine synthesis.

Protein synthesis does not discriminate between selenomethionine and methionine; both of these will be incorporated just the same in muscle an other structural proteins. However, polyamines can be formed only using methionine; the amino acid selenomethionine simply will not work. In a addition to it not even being a substrate for polyamine synthesis, it goes one step further by inhibiting methionine adenosyltransferase:

Selenomethionine will decrease the growth of rapidly-proliferating tumor cells while having no cytotoxic effect on normal cells, just like methylglyoxal. I think this is exactly what you'd expect from polyamine starvation:

As far as I'm concerned, selenomethionine will naturally lower polyamine concentrations in the body starting with the most rapidly-dividing cells first; selenomethionine should work synergistically with methylglyoxal since these do two different and unrelated things, yet both tending towards the same end: One inhibits polyamine synthetic enzymes and the other lowers the concentration of arginine—a polyamine (and prostaglandin) proto-substrate—by transforming it into a cyclic imidazalone.

[1] Witherington, R. "Decreased incidence of prostate cancer with selenium supplementation: results of a double-blind cancer prevention trial." British journal of urology (1998)
[2] Redman, C. "Involvement of polyamines in selenomethionine induced apoptosis and mitotic alterations in human tumor cells." Carcinogenesis (1997)
[3] Redman, Claire, et al. "Inhibitory effect of selenomethionine on the growth of three selected human tumor cell lines." Cancer letters (1998)
[4] Porter, C. "Growth inhibition by methionine analog inhibitors of S-adenosylmethionine biosynthesis in the absence of polyamine depletion." Biochemical and biophysical research communications (1984)​

 

[X3CyO]

It does have a proline, making it more enzymatically-resistant. If anyone doubts that peptides of this length are routinely detected after food consumption, and in all test subjects, I think they'd be forced to reconsider after reading this article:

Pennington, C. "Detection of gluten exorphin B4 and B5 in human blood by liquid chromatography-mass spectrometry/mass spectrometry." The Open Spectroscopy Journal (2007)​

I have a blender that I've used in the past and still sometimes use it to this day. I recently have blended kale and then strained it, produces a fluid having a nice emerald green color. Sometimes I add a garlic clove, cayenne pepper, and salt, but I try not to get in the habit of using too much (although Na⁺ should be safe in people also consuming potassium—the counterion—in high amounts.) Enzymes can be denatured with salt and also with heat. The conventional line of thought is that this doesn't matter one bit, as food enzymes would be destroyed in the stomach anyway on account of them being proteins. But this is not always the case, as it has been proven that bromelain can be absorbed intact with full retention of activity:

Castell, J. "Intestinal absorption of undegraded proteins in men: presence of bromelain in plasma after oral intake." American Journal of Physiology-Gastrointestinal and Liver Physiology (1997)​

But it could be argued that this is unusual for a protein, on account of bromelain being an acid-stable protease. Pepsin and trypsin are acid-stable proteases and necessarily must survive digestion (and all the while without digesting themselves, which some proteolytic enzymes will actually do). I would have to agree with that reasoning, and many proteins do appear to be hydrolyzed almost completely. However: the process of homogenation has been shown to encapsulate proteins inside of liposomes, protecting it from pepsin and facilitating absorption in the jejunum–duodenum (in the case of xanthine oxidase in homogenized milk). Mixing fat with globular proteins can create new food matrix effects which inhibit natural digestion, and cooking can further modify proteins to make them more resistant to pepsin (but also more digestible, depending on the protein and type of cooking). The most research in this area is on starch, seemingly because food industries are interesting in the structural properties of different conformations of starch—these changing greatly whether it's found in the crystalline or in the gelatinized state. There is that classic Pottenger Cat experiment, resulting in the cats being fed raw milk faring better (It could be more alarming to see a modern version using ultra-pasteurized homogenized milk, with recombinant bovine growth hormone, and the fourfold increase in IGF-1 that can induce.)

Pottenger, F. "The effect of heat-processed foods and metabolized vitamin D milk on the dentofacial structures of experimental animals." American journal of orthodontics and oral surgery (1946)​

I think blending is fine because it retains the great majority of the molecular structure of the native fruit/vegetable. Juicing is defined as the separation of the pulp, which may or may not be beneficial. (Humans actually digest the majority of cellulose and hemicellulose they consume, resulting in butryric acid:)

Holloway, W. "Digestion of certain fractions of dietary fiber in humans." The American journal of clinical nutrition (1978)​

And these are calories not normally accounted for in food nutrition tables.

how many calories are generated from a gram of fiber?

Do you know why eating a lot of greens can cause headaches in some? Is it something to do with this mucoid plaque gunk?

 

[Travis]

Apologies.

Sorry. I had flashbacks of the time I had to look-up glutamine concentrations. This amino acid, along with asparagine, is never listed on standard amino acid charts; glutamine concentrations are actually surprisingly hard to come by. The reason for this is simple and straightforward: Acid hydrolysis releases ammonia from glutamine, transforming it into glutamate in the process. This happens during seed germination and is why seeds store extra nitrogen as glutamine or asparagine:

glutamine + HCL + H₂O ⟶ NH₄⁺ + glutamate + H⁺​

Acid hydrolysis of proteins is done to liberate amino acids before they can be sequenced. The characterization of a specific amino acid composition of a protein is ironically confounded by the very process intended for facilitating it.

I would estimate that roughly 97% of all amino acid studies do not explicitly list glutamine or asparagine concentrations, making this actually a difficult thing to know. In nearly all cases, glutamine becomes listed under the amino acid it transforms into. This means it's not entirely correct to say that 'standard amino acid charts do not list glutamine;' they do in fact list glutamine, in a way, but under the heading 'glutamate.' Of course it's impossible to know how glutamate had originally been glutamine before hydrolysis, but plants characteristically store extra nitrogen as either glutamine or asparagine; so knowing the species of the plant is usually enough to find-out whether it would be expected to be high in glutamine or high in asparagine. This is important, as one enzyme (glucosamine-6-phosphate transferase) in the crucial chitin synthetic pathways of C. albicans can use only glutamine explicitly. Wheat is a glutamine-storing plant, as can be verified by looking at a characteristic wheat seed-storage protein (α-gliadin):

Now let's take a look at your standard beef muscle protein (α-actinin):

Admittedly, it does have some glutamine; but most proteins do. There is also the free intracellular glutamine in cells to account for, but as this exists in it's free state you don't need the confounding acid hydrolysis step to (not) determine it. So free glutamine is actually easily to know, yet turns-out to be insignificant. In human skeletal muscle it has been measured at 22.64 μmol/L (3.308·mg/kg),⁽¹⁾⁽*⁾ and fermented sausage before fermentation it is found to 168.6 mg/kg.⁽²⁾ The glutamate levels on the other hand are expressed in grams per kilogram levels (~6.33 g/kg),⁽³⁾ or roughly 2000 times higher than what is found in human skeletal muscle. All other amino acids are also expressed in grams per kilogram levels, and this can be verified through standard amino acid charts.

So how much glutamine is in beef exacly? Is it any higher than egg albumin (below)?

I don't think that beef is particularly high in glutamine; if it was, I wouldn't expect the authors of the articles that purport it to be to actually know this with any certainty. It seems as though their only reason for including beef on the list of 'high-glutamine foods' is because it's high in protein in general. Here is just the first quote that I'd found after I had Googled the term 'foods highest in glutamine:'

'The dietary sources of glutamine includes especially the protein-rich foods like beef,chicken, fish, dairy products, eggs, vegetables like beans, beets, cabbage, spinach,carrots, parsley, vegetable juices and also in wheat, papaya, brussel sprouts, celery, kale and fermented foods like miso.' ―atlantamedicalinstitute.com​

Everything but the kitchen sink is included on the list, and I think it would be more appropriate to concentrate on the foods characteristically high in glutamine per total amino acids: Notably, seeds from plant species which incorporate very high levels of glutamine in its seed-storage proteins. This quote above was from a ghost writer, and ghost writers usually spend more time ghost-plagiarizing articles written by other ghost writers while caring little about veracity. [Ask me how I know.] Most of them don't even read scientific articles at all, and most of the ones that actually do limit themselves to the abstracts. Show me a ghost writer that reads Materials & Methods sections and I'll show you my pet leprechaun.

Does beef deserve to be noted as being relatively high in glutamine per total amino acids? Perhaps maybe a bit above average, but who on Earth is in a position to say with any certainty? In any case, the glutamine concentrations per total amino acids in skeletal muscle is certainly far less than that found in seed-storage proteins of certain plants. This is easy, as only a few are known for this: oats, rye, wheat, and barley are the ones to avoid (although rice needs to be examined). Tomatoes are the one fruit with potentially dangerous amounts of glutamine, and bananas are the one with potentially yeast feeding glucosefructose ratio. Is it any wonder why these two fruits are the only ones usually excluded on the 'don't eat' lists of popular candida diets, although they never explain why (hint: it has something to do with chitin).

Enzymatic hydrolysis followed by high pressure liquid chromatography can accurately determine glutamine concentrations but enzymatic hydrolysis is less reliable since proline bonds are notoriously enzyme-resistant. Accurate glutamine determinations are also not commonly done because glutamine is not an essential amino acid and can be formed from glutamate within the body. Infrared spectroscopy can also determine glutamine levels but these instruments are far less common than HPLC columns and thus less-commonly employed (not to be confused with HPLC-IR).

[1] Hammarqvist, F. "Addition of glutamine to total parenteral nutrition after elective abdominal surgery spares free glutamine in muscle, counteracts the fall in muscle protein synthesis...." Annals of surgery (1989)
[2] DeMasi, T. "Non-protein nitrogen (NPN) and free amino acid contents of dry, fermented and nonfermented sausages." Meat Science (1990)
[3] Wattanachant. "Composition, color, and texture of Thai indigenous and broiler chicken muscles." Poultry science (2004)
[*] 22.64·μmol/L × 146.14·g/mol = 3308.6·μg/L = 3308.6·μg/kg = 3.308·mg/kg ​

 

[sladerunner69]

//

I think this was originally intended by Ray Peat to correct the amino acid imbalance of muscle, moving this towards what a true carnivore would get by reincluding the connective tissue fraction. Gelatin has the Fernstrom competitors phenylalanine, leucine, isoleucine, and tyrosine yet contains no tryptophan; hence, gelatin would be expected to lower brain serotonin when eaten with steak—relative to eating steak alone—but of course less so than than the more concentrated 'branched chain amino acids.' But unlike BCAAs, gelatin provides the amino acids suitable for procollagen synthesis and you can buy it at most any grocery store. Gelatin itself is unbalanced and loses its original justification when eaten in the absence of meat; and for this reason, I don't normally eat gelatin (although I might give it a try one of these days.)

Gelatin is itself unbalanced so what exactly does this mean to you? That it could be detrimental by lowering serotonin and raising dopamine too much?

 

[Wagner83]

I wasn't sure where to post this. I tried bromelain with gelatin and have felt terrible all day, not hungry and very lethargic , slow, like a 6 ft flaccid wiener trying to stand upright.

 

[LeeLemonoil]

Someething on Selenium, they put three differentSe-complexes into their supplement with the reasoning either protects against / fights cancer via different mechanism
Selenium Forms Protect Against Cancer | Life Extension

Curiously, no mention of Selenocystathione which I thought was very beneficial and has a ot of research backing it.


And stumbled across this:
Computational genomic analysis of hemorrhagic fever viruses. Viral selenoproteins as a potential factor in pathogenesis. - PubMed - NCBI
Interesting, I remember reading somewhere that recent Ebola outbreak was in regions with low selenium soils
Computational genomic analysis of hemorrhagic fever viruses. Viral selenoproteins as a potential factor in pathogenesis.
Review article
Ramanathan CS, et al. Biol Trace Elem Res. 1997.
Show full citation
Abstract
A number of distinct viruses are known as hemorrhagic fever viruses based on a shared ability to induce hemorrhage by poorly understood mechanisms, typically involving the formation of blood clots ("disseminated intravascular coagulation"). It is well documented that selenium plays a significant role in the regulation of blood clotting via its effects on the thromboxane/prostacyclin ratio, and effects on the complement system. Selenium has an anticlotting effect, whereas selenium deficiency has a proclotting or thrombotic effect. It is also well documented that extreme dietary selenium deficiency, which is almost never seen in humans, has been associated with hemorrhagic effects in animals. Thus, the possibility that viral selenoprotein synthesis might contribute to hemorrhagic symptoms merits further consideration. Computational genomic analysis of certain hemorrhagic fever viruses reveals the presence of potential protein coding regions (PPCRs) containing large numbers of in-frame UGA codons, particularly in the -1 reading frame. In some cases, these clusterings of UGA codons are very unlikely to have arisen by chance, suggesting that these UGAs may have some function other than being a stop codon, such as encoding selenocysteine. For this to be possible, a downstream selenocysteine insertion element (SECIS) is required. Ebola Zaire, the most notorious hemorrhagic fever virus, has a PCR with 17 UGA codons, and several potential SECIS elements can be identified in the viral genome. One potential viral selenoprotein may contain up to 16 selenium atoms per molecule. Biosynthesis of this protein could impose an unprecedented selenium demand on the host, potentially, leading to severe lipid peroxidation and cell membrane destruction, and contributing to hemorrhagic symptoms. Alternatively, even in the absence of programmed selenoprotein synthesis, it is possible that random slippage errors would lead to increased encounters with UGA codons in overlapping reading frames, and thus potentially to nonspecific depletion of SeC in the host.

 

[LeeLemonoil]

Will there ever be a book from Travis where he/you organize and conceptionalize your ingenious findings in a more accesible form than trying to follow all your forum posts ?
I for one am prepared to pay the deserved money for it or participate in crowdfundig or stuff.

 

[YourUniverse]

Travis, do you know if mucuna pruriens requires cycling? Will a tolerance develop?

 

[Amazoniac]

My Nutritional Science Blog

I just came across another instance of The Steinbeck:

'Class-I helical cytokine genes are scattered over the genome of mice and men, where they are found mostly isolated. Some occur in small aggregations of two or sometimes three genes.' ―Huising​

I wouldn't bother with this article despite it's intriguing name; he talks more about cytokine and receptor structure than he talks about their evolutionary development. Apparently: cytokines haven't been examined thoroughly enough across taxa to know much about which had came first during evolution, and he ends-up talks mainly about the cytokines of fish (for some reason, but perhaps because they are most studied). Besides the mind-numbing triteness of the phrase, his fixation on aquatic species makes the use of The Steinbeck doubly inappropriate; he should have resisted that temptation, sidelined the delusional notion that he was actually being original and witty, spared us from the mental image of John Malkovich petting a fμcking bunny to death, and had just used the gοddamn Reverse Steinbeck like any decent person would! Even the following would have been acceptable:

'Class-I helical cytokine genes are scattered over the genome of fish and men, where they are found mostly isolated. Some occur in small aggregations of two or sometimes three genes.' ―Huising
​

[By substituting Greek letters a person can get by with using profanity: The lowercase mu (μ) is good for the foregoing four-letter and also signifies micro (10⁻⁶)—or that is, οne-in-a-milliοn (the letter gamma (γ) also had been used for this, historically, but had been made obsolete in the '50s)—and the lowercase omicron (ο) is distinguishable only by computers. To demonstrate this: can tell me how many omicrons I've embedded within this comment without using a computer?]

Huising, M. "Phylogeny and evolution of class-I helical cytokines." Journal of Endocrinology (2006)​

 

[Blossom]

Two?

 

[SB4]

@Travis I have CFS / POTS / Gastroparesis. I have generally very poor appetite. I recently noticed after 5 weeks with no ejaculation, around week four I notice my stomach starts growling slightly again between meals (it hasn't done this in years) and my appetite significantly improved. However after I ejaculated, it went more or less back to normal low appetite. I have noticed a similar effect with other periods of abstinence.

I think I could be deficient in a certain mineral or hormone that is in semen that is also required for gastric acid production. Zinc is obviously the main contender as it is used in carbonic anhydrase required to produce HCl, and it is 3% RDA in semen.

The other big one is copper though I'm not sure how that relates to gastric acid, also at 3%.

I suspect I would have obtained the deficiency via dysautonomia -> gastroparesis -> poor absorption -> low zinc (or other mineral or amino acids) -> low stomach acid -> low zinc (or other mineral or amino acids) absorption, vicious circle.

My only other thought is that prolactin rises and acetylcholine testostorone, etc drops. Perhaps because my health is in such a shocking state it takes a while for these hormones to build back up? I should also mention my libido is low to very low.

You are good at analyzing these sought of things. Any ideas?

 

[Travis]

//


Gelatin is itself unbalanced so what exactly does this mean to you? That it could be detrimental by lowering serotonin and raising dopamine too much?

I think it loses it's original justification when not accompanied by meat, but that's not to say that it should be avoided otherwise. It does have collagen's amino acids so it could be a really good idea—along with vitamin C—for healing sprains. It does have small amounts of serotonin's competing amino acids, so I think gelatin could be worth experimenting with also in that regard. I think I might pick it up from the grocery store one of these days but as of yet I have little experience with it.

 

[Travis]

I wasn't sure where to post this. I tried bromelain with gelatin and have felt terrible all day, not hungry and very lethargic , slow, like a 6 ft flaccid wiener trying to stand upright.

I'm sure you had given yourself a bolus dose of free amino acids; bromlain is so notorious for hydrolyzing gelatin that pineapple is contraindicated in the preparation of Jello™ due to it's collagenase activity—which you can frickin' see! I have seen this—and the enzyme activity of the extracts is even commonly reported in gelatin digestion units (GDU). I am not sure what to make of this, but it could have something to do with the sympathoinhibitory effects of glycine.

 

[Travis]

Someething on Selenium, they put three differentSe-complexes into their supplement with the reasoning either protects against / fights cancer via different mechanism
Selenium Forms Protect Against Cancer | Life Extension

Curiously, no mention of Selenocystathione which I thought was very beneficial and has a ot of research backing it.


And stumbled across this:
Computational genomic analysis of hemorrhagic fever viruses. Viral selenoproteins as a potential factor in pathogenesis. - PubMed - NCBI
Interesting, I remember reading somewhere that recent Ebola outbreak was in regions with low selenium soils
Computational genomic analysis of hemorrhagic fever viruses. Viral selenoproteins as a potential factor in pathogenesis.
Review article
Ramanathan CS, et al. Biol Trace Elem Res. 1997.
Show full citation
Abstract
A number of distinct viruses are known as hemorrhagic fever viruses based on a shared ability to induce hemorrhage by poorly understood mechanisms, typically involving the formation of blood clots ("disseminated intravascular coagulation"). It is well documented that selenium plays a significant role in the regulation of blood clotting via its effects on the thromboxane/prostacyclin ratio, and effects on the complement system. Selenium has an anticlotting effect, whereas selenium deficiency has a proclotting or thrombotic effect. It is also well documented that extreme dietary selenium deficiency, which is almost never seen in humans, has been associated with hemorrhagic effects in animals. Thus, the possibility that viral selenoprotein synthesis might contribute to hemorrhagic symptoms merits further consideration. Computational genomic analysis of certain hemorrhagic fever viruses reveals the presence of potential protein coding regions (PPCRs) containing large numbers of in-frame UGA codons, particularly in the -1 reading frame. In some cases, these clusterings of UGA codons are very unlikely to have arisen by chance, suggesting that these UGAs may have some function other than being a stop codon, such as encoding selenocysteine. For this to be possible, a downstream selenocysteine insertion element (SECIS) is required. Ebola Zaire, the most notorious hemorrhagic fever virus, has a PCR with 17 UGA codons, and several potential SECIS elements can be identified in the viral genome. One potential viral selenoprotein may contain up to 16 selenium atoms per molecule. Biosynthesis of this protein could impose an unprecedented selenium demand on the host, potentially, leading to severe lipid peroxidation and cell membrane destruction, and contributing to hemorrhagic symptoms. Alternatively, even in the absence of programmed selenoprotein synthesis, it is possible that random slippage errors would lead to increased encounters with UGA codons in overlapping reading frames, and thus potentially to nonspecific depletion of SeC in the host.

Did they explain why selenium is associated with increased blood clotting? If I were to make a guess, I'd say that having reduced levels of glutathione peroxidase—which is dependent on selenocysteine—would increases the concentrations of all prostaglandins and specifically thromboxane A₂: the prostaglandin so peculiar in it's platelet-aggregating and prothrombic properties that it'd been named for it. There are many such selenoenzymes and one of them—glutathione peroxidase №4—carries out the task of transforming lipid peroxides into lipid alcohols. But more importantly: The main form of this enzyme can transform peroxynitrite into nitrite in the presence of reduced glutathione. Peroxynitrite is the the other substrate besides arachidonic acid for the enzyme cyclooxygenase; it has been shown that prostaglandin H₂ concentations are a direct function of cyclooxygenase, arachidonic acid, and peroxynitrite concentations.

 

[Fractality]

@Travis - I don't know how you can stomach a blended pineapple smoothie even with an added banana. It's so bitter! I had some leftover pineapple slices this morning and blended them with unpasteurized orange juice and nonfat milk powder. I couldn't finish it due to the bitterness.

 

[Travis]

Will there ever be a book from Travis where he/you organize and conceptionalize your ingenious findings in a more accesible form than trying to follow all your forum posts ?
I for one am prepared to pay the deserved money for it or participate in crowdfundig or stuff.

I am going to write my first article pretty soon here and I'll let you know when it's done (and I hope that you'll like it).