Amino Acid Supplementation For People With Poor Digestion

[haidut]

Guru, I went for a more careful read of your previous classes on this minimum requirement. Here's one of the publications that thou post'd:

- Dietary Methionine Restriction Increases Fat Oxidation in Obese Adults with Metabolic Syndrome

It's interesting. Hopefully divine forces draw Daniel Wich here for him to opine about the 'plasma methionid' test.

Anyway, your experiment led me to everything that follows..


From what I understand, below they used a method that judges sufficiency by enough protein synthesis when the required amino acids are present. If there are missing ones, those that is in excess will disposed by burning them for energy. They pick phenylalanine for this purpose and radiolabel a part of it to detect its excretion (that should've been incorported instead).

- Total sulfur amino acid requirement in young men as determined by indicator amino acid oxidation with l-[1-13C]phenylalanine

"Total sulfur amino acids (SAAs) are the first limiting amino acids in several foods (9); therefore, knowledge of the mean requirement and population-safe intake of SAAs is important for making recommendations about protein and amino acid intakes in humans."

"[..]because nitrogen balance tends to underestimate nitrogen losses and is influenced by excess energy intake, amino acid requirements are susceptible to underestimation (12–16)."

"The first published estimates of total SAA requirements were based on the nitrogen balances of 6 men (11). The current population-safe intake of SAAs for adults recommended by the FAO/WHO/UNU is 13 mg·kg−1·d−1 (10), which is based on the highest estimated individual requirement to achieve positive nitrogen balance in studies carried out by Rose et al (11) in men and by Reynolds et al (36) in women. Human nutrient requirements, except for energy, are set according to a statistical model that uses the mean requirement plus 2 SDs to determine a population-safe intake for a given nutrient (37). In nitrogen balance studies used to estimate total SAA requirements, one can easily calculate a mean requirement and an SD because individual data are provided for each of the 6 subjects in the original paper by Rose et al (11). When we recalculated this nitrogen balance data, we found a mean requirement of 13.2 mg·kg−1·d−1. To this new mean, we added 2 times the SD to arrive at an estimated population-safe total SAA intake of 18 mg·kg−1·d−1. This value is similar to the population-safe intake found in the present study (21 mg·kg−1·d−1) and is consistent with the 24-h balance estimates discussed below (17,38)."

"Given the complexity of SAA metabolism, estimating total SAA requirements by direct oxidation tracer methods is extremely difficult. This is because the carboxyl carbon of methionine is not directly lost to the bicarbonate pool, nor is it irreversibly oxidized to carbon dioxide during degradation; a condition that must be met for the principles of direct oxidation to apply (15). However, Young et al (17) suggested that the current FAO/WHO/UNU population-safe SAA intake of 13 mg·kg−1·d−1 is too low on the basis of 24-h balance studies using l-[methyl-2H3,1-13C]methionine as a tracer. In that study, 5 men were fed 13 mg SAAs·kg−1·d−1 and tracer oxidation was monitored over 24 h. Although all of the subjects did not achieve balance at that intake, some subjects were close enough to zero balance for the authors to conclude that the true mean total SAA requirement was not much different from the FAO/WHO/UNU population-safe intake (17). The authors also suggested that for all subjects to achieve methionine balance, the population-safe intake should be set at ≈25 mg·kg−1·d−1. These results were confirmed in a later study (38)."

"IAAO is an independent method of estimating indispensable amino acid requirements in humans. Since its first applications in humans (23), IAAO has evolved into a relatively noninvasive and efficient means of elucidating the indispensable amino acid needs of children and adults (26,28). The technique monitors the oxidation of an independent, indispensable indicator amino acid in response to graded intakes of an indispensable test amino acid. As the intake of the test amino acid approaches its requirement, the oxidation of the indicator decreases such that further increments in the test amino acid will have no effect on the oxidation of the indicator amino acid (25)."

"In the present study, we found a mean total SAA requirement of 12.6 mg·kg−1·d−1, with a population-safe intake of 21.0 mg·kg−1·d−1. This latter amount is 60% greater than the current recommended total SAA requirement of 13.0 mg·kg−1·d−1 (10). Both the mean and safe IAAO-determined values agree with values predicted from 24-h balance data (17,38) and values recalculated from early nitrogen balance data (11). We conclude that 12.6 mg·kg−1·d−1 is a reasonable estimate of the average SAA requirement (37,40). Setting a dietary reference intake for total SAAs will depend on the analysis of more individual data, which may modify our current estimated population requirement of 21 mg·kg−1·d−1."

"Ensuring adequate B-vitamin nutriture when attempting to study SAA metabolism is of the utmost importance."

"Each subject randomly received each of 6 dietary methionine intakes: 0, 6.5, 13.0, 19.5, 26.0, and 32.0 mg·kg−1·d−1. Each study consisted of a 2-d adaptation period to a prescribed diet. The diet provided 1.0 g protein·kg−1·d−1 and was followed by a single study day on which phenylalanine kinetics were measured with the use of l-[1-13C]phenylalanine at 1 of the 6 dietary methionine intakes and a crystalline amino acid intake of 1.0 g·kg−1·d−1. The dietary study periods were separated by ≥1 wk; all subjects completed all 6 studies within 3 mo."

View attachment 13705​

There's a cavern by them that it's possible for others needs to not be met in spite of the adequate protein synthesis, but the experiment was on requirements for methionine dispensing the need for cysteine. When cysteine is not present, the mean minimum requirement of these pimps was about 12.5 mg/kg/d, and more (21 mg/kg/d) if they was to cover most people (just like it happens when you have to generalize recommendations for a larger population). If both are present, needs should be reduced.

The next publication is the 2 mg/kg/d experiment that seems to be the source of your suggestion. It was on people dealing with cancre and the restriction was a form of starvation where tumors are more impacted than the person, and this should have an overall positive effect.

- Nutrient Intake and Nutritional Indexes in Adults With Metastatic Cancer on a Phase I Clinical Trial of Dietary Methionine Restriction

"Although [methionine's regenerating] enzymes [dependent on folate/cobalamin and betaine] are functional in some tumors (4), most tumors are dependent on exogenous, preformed methionine and, therefore, fail to grow, even in the presence of homocysteine (5–8)."

"The selective antitumor activity of methionine restriction is not due to an absolute difference between benign and malignant tissues, because neither can survive for long in the complete absence of methionine. Rather, tumors are more sensitive than normal tissues to methionine restriction; just as many tumors are more sensitive to chemotherapy and radiation therapy. In contrast, restriction of other essential amino acids is either very toxic or ineffective (19). Methionine restriction, therefore, does not represent indiscriminate 'starvation.'"

"The protocol for implementing the dietary methionine restriction was modified over the course of the study to develop a dietary pattern that could best be used by free-living cancer patients. All patients were placed on Hominex-2 Amino Acid-Modified Medical Food (Ross Products Division, Abbott Laboratories, Columbus, OH), which is approved for treatment of patients with homocystinuria (Table 2). Hominex-2 contains essentially no methionine (Table 3). The quantity of Hominex-2 consumed daily by each patient was calculated to provide 0.6–0.8 g protein/kg body wt. Hominex-2 dose and energy intake were maintained at baseline levels throughout participation, rather than reduced as patients lost weight. Hominex-2 served as the primary dietary protein source for all patients."

Spoiler

View attachment 13707 View attachment 13708

"Weight loss was the only side effect of the diet, and all but one patient regained weight on resumption of a normal diet. The only patient who failed to regain weight after discontinuing the study had cancer cachexia related to pancreatic adenocarcinoma even before his enrollment. Plasma methionine levels and food records indicated that patients adhered to the diet."

"After observing weight loss in Patients 1–4, we refined the diet to provide increased energy and protein intake. Nonetheless, Patients 5–8, who maintained energy intakes considerably above baseline and protein intakes above the RDA, still lost weight at the same rate as Patients 1–4. One possible explanation for this observation is that 35 kcal/kg/ day, which was consumed by Patients 5–8, was still inadequate to maintain positive nitrogen balance. This possibility is supported by early studies showing that energy requirements are considerably higher for patients whose sole nitrogen source consists of purified amino acids than for those who consume intact proteins (21)."

"Alternatively, weight loss experienced by patients in the trial may have been independent of energy intake but, rather, attributable to 'obligatory' muscle catabolism related to methionine restriction per se. A recent study designed to quantify dietary methionine requirements in normal subjects sheds light on this issue (22). In that study, stable isotope methods were used to measure obligatory methionine oxidation in normal subjects on a diet completely devoid of sulfur amino acids (methionine and cysteine) for 5 days. Although somewhat controversial (23), obligatory oxidation rates are considered by many to represent the minimum requirement for amino acids, that is, the amount that is oxidized despite maximal body conservation. The obligatory oxidative loss of methionine was 13 mg/kg/day in that study (22). Patients in our trial, who were restricted to 2 mg methionine/kg/day, therefore, consumed 11 mg/kg/day less than the minimum requirement. However, they consumed adequate amounts of cysteine, which is present in Hominex-2. They therefore may have had obligatory methionine oxidation rates 13 mg/kg/day. The fact that all patients reversibly lost weight, despite what would normally be considered adequate energy and protein intake, may actually be encouraging, since it confirms that patients adhered to the diet. The basic premise of this strategy is that dietary methionine restriction will have a greater deleterious effect on tumors than on normal host tissues."​

It wasn't low in cysteine. You'll find various other experiments that require methionine restriction using that product (Hominex-2 by Abbott), and its composition makes up for the lowered methionine content. It's the opposite of casein, that happens to be high in methionine and low in cysteine. Check this out:

View attachment 13709​

Therefore I don't think it's a reliable reference for minimum requirements.

Regarding this sparing effect..

- Dietary cysteine reduces the methionine requirement in men

"The current FAO/WHO/UNU population-safe intake of total sulfur amino acids (SAAs) in healthy adults, based on early nitrogen balance studies (1–3), is 13 mg·kg−1·d−1 (4). We previously reported that this value is 60% lower than the population-safe intake found in a study of men by indicator amino acid oxidation (IAAO) (5[↑↑]). Using l-[1-13C]phenylalanine as an indicator, we found that the mean methionine requirement of 6 men in the absence of dietary cysteine was 12.6 mg·kg−1·d−1 and the upper limit of the 95% CI of this mean, which is an estimate of the population-safe intake, was 21 mg·kg−1·d−1 (5). Recent studies of SAA kinetics in humans confirmed, with the use of labeled methionine tracers (6,7), that the current FAO/WHO/UNU recommendations for total SAA intake (4) are too low. In addition, using individual data provided in the early nitrogen balance study by Rose et al (1), we recalculated the mean and population-safe intake of total SAAs to be 13.2 and 18 mg·kg−1·d−1, respectively. Both of these recalculated values are similar to those found in our previous IAAO study (5) and further confirm that the population-safe intake of SAA is greater than the published FAO/WHO/UNU value of 13 mg·kg−1·d−1 (4)."

"The ability of cysteine to reduce the quantitative requirement for methionine in humans was reported in early studies (2,8–10). In contrast, a more recent series of reports on methionine kinetics using methionine and cysteine tracers suggests that cysteine has no sparing effect on methionine requirements in humans (7,11–15). However, the failure to detect a sparing effect in these recent experiments may have resulted from the investigators unknowingly supplying inadequate dietary SAA intakes. The test diets adopted in these kinetic studies were based on the FAO/WHO/UNU estimates, which we (5) and others (6,7) maintain are too low. To detect a cysteine sparing effect on methionine requirements, cysteine must be present in amounts adequate to completely, or largely, arrest the flow of metabolites through the transsulfuration pathway, whereas methionine must be present in amounts adequate to meet all its other metabolic functions, including protein synthesis, transmethylation, and the provision of homocysteine for remethylation reactions necessary for folate and betaine metabolism. Unless the total SAA needs of all subjects are met, addition of cysteine to the diet will lead to an immeasurably small sparing effect on methionine requirements (13,14)."

"Each subject randomly received each of 6 dietary methionine intakes: 0, 2.5, 5.0, 7.5, 10.0, and 13.0 mg·kg−1·d−1. Dietary cysteine was held constant at an intake of 21 mg·kg−1·d−1. Each study consisted of a 2-d adaptation period to a prescribed diet (17). The diet provided 1.0 g protein·kg−1·d−1 and was followed by a single study day on which phenylalanine kinetics were measured with the use of l-[1-13C]phenylalanine at 1 of the 6 dietary methionine intakes and a protein intake of 1.0 g·kg−1·d−1. The study dietary periods were separated by ≥1 wk; all subjects completed all 6 studies within 3 mo."

"In the current experiment we found a mean methionine requirement of 4.5 mg·kg−1·d−1 and a population-safe intake of 10.1 mg·kg−1·d−1 when cysteine was fed at an excess of 21 mg·kg−1·d−1."

View attachment 13710
Less methionine to reach the breakpoint this time, so needs are reduced and lower amounts are enough to prevent other amino acids from being wasted.

"The evidence in support of cysteine having a sparing effect on methionine requirements in humans and animals is substantial. As early as 1941, Womack and Rose (8) showed a 17% sparing effect of cysteine on methionine requirements in rats when growth rates were used as an indicator. Shortly thereafter, a series of nitrogen balance studies in men and women showed a sparing effect ranging from 48% to 89% (2,9,10). In addition to these studies, subsequent studies showed that dietary cysteine suppresses transsulfuration in rats (26,27) and humans (11), thus providing a metabolic basis for the sparing effect of cysteine on methionine requirements."

"The available evidence indicates that the sparing effect of cysteine is based on a repartitioning of homocysteine between competing pathways. Although no change appears to occur in the rate of homocysteine remethylation to methionine by either of the available remethylation pathways (11,26,27), there is a clear reduction in the rate of transsulfuration. The net result is that the fractional remethylation of homocysteine increases while that portion metabolized by transsulfuration decreases."​

The protein consumption in these experiments wasn't extreme, around the 0.8 g/kg/d standard recommendation and up to 1 g. I'm mentioning this because I was wondering if it wasn't a matter of having shoved down amino acids on these guys and increasing their requirement for methionid along.

There were subjects needing more or less but the mean value was 4.5 mg/kg/d conditioned to the higher cysteine intake. I'm not aware of foods being able to provide this much cysteine without methionine.

It seems to me that the 2 mg/kg/d value is too low even for cultures that eat little animal protein, are skinny and small, simpler lives, no stimulants, low calories, and so on; all supportive for reducing the need for it. According to such figure, a person weighing 55 kg would require at least 110 mg, but they certainly obtain this from diet, possibly more than double, making it difficult to judge how low you can go without issues.

Contrary to that, liver challenges, military stress, generalized malnutrition making the person unable to compensate for the lack of methionine, wasting, etc, should all increase the requirements above normal.

I'm sure you remember the quotes below, they mention the accumulation, yet in some cases still find it useful to give more.

- Treatment Of Cirrhosis Of The Liver By A Nutritious Diet And Supplements Rich In Vitamin B Complex

"although the choline and methionine content in the cirrhotic liver may be normal or actually higher than normal,[8a] these factors are not available for utilization"

"Experimental studies demonstrated that an inadequate level of methionine cannot be compensated for by excessive levels of choline and cystine.[10] It was further demonstrated that when methionine was added to choline in experimental hepatic damage and growth, a 50 per cent improvement in therapeutic results occurred.[10,15] The damaged liver thus appears to have lost its transmethylation ability and requires both synthetic methionine and choline until normal transmethylation can take place from the ingested food."

"It has been suggested that the lipotropic agent methionine could enhance in a synergistic way the lipotropic (or fatty-cirrhosis-preventing) activity of choline.[7] Animal experiments revealed further that in hepatic damage choline would largely prevent the cirrhosis but not the necrosis and hemorrhage. Methionine was found to effectively prevent both types of damage to the liver. Experimental studies also showed that the cirrhotic symptoms due to choline deficiency result from lack of a methyl-containing essential other than choline and that methionine can directly supply this lack.[8] It is now apparent that although diets may contain an adequate supply of choline, an imbalance or deficiency of other dietary constituents can nullify the lipotropic action of the choline.[9]"

"The high protein diet which I prescribed consisted not only of a high casein source of proteins by the use of skimmed milk feedings and cottage cheese but also of servings of meat three times a day wherever possible. The importance of a high protein diet in cirrhosis of the liver is now thoroughly established[13] and takes precedence over dietary carbohydrate in therapeutic importance. The maximum use of meat in this diet appeared to be advisable because of the necessity for providing the essential amino acids which contain the basic methyl groups, with and without the sulfur radical. These methyl groups are required by the liver for the transmethylation function which institutes regeneration and healing in cirrhosis. As has previously been stated, cirrhosis of the liver when produced experimentally is now regarded as a methyl-group deficiency disease."

"Second, in a controlled series of 62 patients over an eight year period,[11] therapeutic results suggested that the combination of methionine and choline resulted in a better therapeutic response than did various other combinations of amino acids, diet, liver and vitamin supplements in the treatment of hepatic cirrhosis. Methionine was taken orally in capsule form, the dosage being 2 Gm. daily. Similarly, choline chloride was administered orally in a daily dosage of 2 Gm.[10d]"​

- Protective CO2 and aging

"The age accelerating effect of methionine might be related to disturbing the methylation balance, inappropriately suppressing cellular activity."​

Collagen should buffer it and avoid the inappropriate effect. Those researchers mentioned gelatin in their articles, they've considered it (and some used it). To me it doesn't look like increasing everything but methionine and choline would lead to better outcomes. Do you think that they would had fared better if these were cut to the minimum consistently? When do you think that more is desirable?

If anything, it's the uncompensated prolonged restriction that is concerning the most:

- Treatment Of Cirrhosis Of The Liver By A Nutritious Diet And Supplements Rich In Vitamin B Complex

"Interestingly, in contrast to pure methionine restriction, combined methionine and choline restriction have prooxidant, proinflammatory effects in the liver [92,93] and may even promote the development of liver cirrhosis [94] and hepatocellular carcinoma [95]. Methionine- and choline-deficient (MCD) diet in mice also induces liver steatosis and may be used as a suitable model for investigation of the pathophysiological mechanisms of NAFLD [96]. In 2 weeks MCD diet induces focal microvesicular liver steatosis, while in 6 weeks inflammation accompanies diffuse micro- to macrovesicular steatosis with increased serum level of C-reactive protein [93]. These changes are associated with increased levels of malondialdehyde and nitrites+nitrates and reduced GSH level, thus indicating that MCD diet causes oxidative and nitrosative stress in the liver. Additionally, the antioxidative capacity of the liver was found to be decreased by MCD diet due to the reduction of superoxide dismutase and catalase activities, the reduction being the most extensive after 4 week-treatment with MCD diet [93]. Lack of methionine and choline in the diet was also found to cause alterations in free fatty acid profile in the liver [92]. Within 2 weeks it causes a decline in palmitic, stearic, arachidonic and docosahexaenoic acid (DHA). The significance of this finding should be further investigated, but a decrease in DHA level may at least partially contribute to the proinflammatory effect of MCD diet on the liver [92]. All of these changes are dominantly caused by choline deficiency. However, although choline deficiency is sufficient for the development of steatosis, both methionine and choline deficiency are essential for the development of inflammation in the liver [97]. These findings clearly indicate, that adequate intake of micronutrients according to daily requirements is a prerequisite for beneficial effects of dietary methionine restriction on metabolic processes and function of the liver."​

As they said in the human study, methionine restriction diet (MRD) are reliable mimics of caloric restriction (CR) and achieve the same lifespan extension. I don't see how MRD would be harmful if it can pull this off. Considering methionine is an essential amino acid, of course if you completely remove it from the diet there will be issues down the road. Until we know more how much methionine is safe (at the upper limit) I would not take any more than what is in the diet. Same applies to cysteine. Just as you mention the evidence for liver damage from lack of methionine, there is also evidence for liver and heart toxicity at increased daily intake too.
Effect of methionine dietary supplementation on mitochondrial oxygen radical generation and oxidative DNA damage in rat liver and heart
"...Methionine restriction without energy restriction increases, like caloric restriction, maximum longevity in rodents. Previous studies have shown that methionine restriction strongly decreases mitochondrial reactive oxygen species (ROS) production and oxidative damage to mitochondrial DNA, lowers membrane unsaturation, and decreases five different markers of protein oxidation in rat heart and liver mitochondria. It is unknown whether methionine supplementation in the diet can induce opposite changes, which is also interesting because excessive dietary methionine is hepatotoxic and induces cardiovascular alterations. Because the detailed mechanisms of methionine-related hepatotoxicity and cardiovascular toxicity are poorly understood and today many Western human populations consume levels of dietary protein (and thus, methionine) 2–3.3 fold higher than the average adult requirement, in the present experiment we analyze the effect of a methionine supplemented diet on mitochondrial ROS production and oxidative damage in the rat liver and heart mitochondria. In this investigation male Wistar rats were fed either a L-methionine-supplemented (2.5 g/100 g) diet without changing any other dietary components or a control (0.86 g/100 g) diet for 7 weeks. It was found that methionine supplementation increased mitochondrial ROS generation and percent free radical leak in rat liver mitochondria but not in rat heart. In agreement with these data oxidative damage to mitochondrial DNA increased only in rat liver, but no changes were observed in five different markers of protein oxidation in both organs. The content of mitochondrial respiratory chain complexes and AIF (apoptosis inducing factor) did not change after the dietary supplementation while fatty acid unsaturation decreased. Methionine, S-AdenosylMethionine and S-AdenosylHomocysteine concentration increased in both organs in the supplemented group. These results show that methionine supplementation in the diet specifically increases mitochondrial ROS production and mitochondrial DNA oxidative damage in rat liver mitochondria offering a plausible mechanism for its hepatotoxicity."

The atherogenic effect of excess methionine intake
"...Mice fed methionine-rich diets had significant atheromatous pathology in the aortic arch even with normal plasma homocysteine levels, whereas mice fed B vitamin-deficient diets developed severe hyperhomocysteinemia without any increase in vascular pathology. Our findings suggest that moderate increases in methionine intake are atherogenic in susceptible mice. Although homocysteine may contribute to the effect of methionine, high plasma homocysteine was not independently atherogenic in this model. Some product of excess methionine metabolism rather than high plasma homocysteine per se may underlie the association of homocysteine with vascular disease."

 

[Amazoniac]

As they said in the human study, methionine restriction diet (MRD) are reliable mimics of caloric restriction (CR) and achieve the same lifespan extension. I don't see how MRD would be harmful if it can pull this off. Considering methionine is an essential amino acid, of course if you completely remove it from the diet there will be issues down the road. Until we know more how much methionine is safe (at the upper limit) I would not take any more than what is in the diet. Same applies to cysteine. Just as you mention the evidence for liver damage from lack of methionine, there is also evidence for liver and heart toxicity at increased daily intake too.
Effect of methionine dietary supplementation on mitochondrial oxygen radical generation and oxidative DNA damage in rat liver and heart
"...Methionine restriction without energy restriction increases, like caloric restriction, maximum longevity in rodents. Previous studies have shown that methionine restriction strongly decreases mitochondrial reactive oxygen species (ROS) production and oxidative damage to mitochondrial DNA, lowers membrane unsaturation, and decreases five different markers of protein oxidation in rat heart and liver mitochondria. It is unknown whether methionine supplementation in the diet can induce opposite changes, which is also interesting because excessive dietary methionine is hepatotoxic and induces cardiovascular alterations. Because the detailed mechanisms of methionine-related hepatotoxicity and cardiovascular toxicity are poorly understood and today many Western human populations consume levels of dietary protein (and thus, methionine) 2–3.3 fold higher than the average adult requirement, in the present experiment we analyze the effect of a methionine supplemented diet on mitochondrial ROS production and oxidative damage in the rat liver and heart mitochondria. In this investigation male Wistar rats were fed either a L-methionine-supplemented (2.5 g/100 g) diet without changing any other dietary components or a control (0.86 g/100 g) diet for 7 weeks. It was found that methionine supplementation increased mitochondrial ROS generation and percent free radical leak in rat liver mitochondria but not in rat heart. In agreement with these data oxidative damage to mitochondrial DNA increased only in rat liver, but no changes were observed in five different markers of protein oxidation in both organs. The content of mitochondrial respiratory chain complexes and AIF (apoptosis inducing factor) did not change after the dietary supplementation while fatty acid unsaturation decreased. Methionine, S-AdenosylMethionine and S-AdenosylHomocysteine concentration increased in both organs in the supplemented group. These results show that methionine supplementation in the diet specifically increases mitochondrial ROS production and mitochondrial DNA oxidative damage in rat liver mitochondria offering a plausible mechanism for its hepatotoxicity."

The atherogenic effect of excess methionine intake
"...Mice fed methionine-rich diets had significant atheromatous pathology in the aortic arch even with normal plasma homocysteine levels, whereas mice fed B vitamin-deficient diets developed severe hyperhomocysteinemia without any increase in vascular pathology. Our findings suggest that moderate increases in methionine intake are atherogenic in susceptible mice. Although homocysteine may contribute to the effect of methionine, high plasma homocysteine was not independently atherogenic in this model. Some product of excess methionine metabolism rather than high plasma homocysteine per se may underlie the association of homocysteine with vascular disease."

Since most people indeed get too much, there should be no problem in having in mind requirements that only a ninja is able to consume.

 

[Amazoniac]

Some more thoughts..

This thread started as an alternative for people dealing with weak protein digestion, so it could be inadvertisingly a lower methionine diet. Since it's a matter of inability to digest and not a specific condition that calls for certain amino acids in particular, it makes more sense to try first the desired protein foods with digestive enzymes instead of resorting to a formula.

I'm not suggesting methionine supplementation and I don't use it on my cynical practice. But we can't separate the methionine from protein when greater intakes are trouted as beneficial.

But hypothesically, what would happen if Georgi started selling Methioban: an effective absorption inhibitor of not only methionine, but also cysteine? This product would keep methionine intake at no more than 2 mg/kg/d because anything beyond ours truly considers detrimental.

But you isn't living on a pristine region with sulfurous crystalline wasser. Your wasser has a few letters in it if observed under a microscope that once combined in the body, they form Mastercard (cake, 2019).
- Acetaminophen (Tylenol) Depletes DHEA-S And Other Sulfated Steroids
Check out the last link as well.

There is no escape: Zeus believes that desirable requirements for choline are also at 2 mg/kg/d, which may be true if you isn't demanding more of it.

Little did your body expect'd that in the meantime 500 mg of nicotinamide was about to be deliver'd all of the sudden. How should it handle it? Should it compromise creatine synthesis? Adopt the Mastercard as pet? But what if the pet gets along with the present estrogen, will there be space for both?

Protein digestion wasn't optimal to begin with, would the amino acid formula finally deplete the cobalamin reserves that were possibly low for not releasing it from food? Protein was escaping digestion before formula use, so lack of cobalamin is pausable (if not from its degradation due to the noxious gases).

You could resort to Energin's B-side.. if it existed. After all, assuming that you're not wasting the other amino acids in the formula or complementing with your own muscles, there will be extra reliance on folate and cobalamin.

But Energin alone should give you a boost and increase your tolerance enough to make you put up with my posts and in reading in more detail, you realize that I forgot to comment that the Hominex-2 product used in the '2 mg/kg/d cancre' experiment had not only extra cysteine, but it also provided about 200 mg of choline from supplementation alone. You'll also notice a gross mistake on my part: it wasn't 0.9% of cysteine/protein, it was 0.9 g of cysteine/30 g of protein, so 3%, and if they took 56 g of protein, that's 1.7 g of cysteine (again, from supplement alone), which is more than the 1.5 g used in the other experiment mentioned.

A third factor is in Diokine's graph: it's more appropriate to judge the compensation thinking more in terms of how many molecules instead of how much (as it was for the graph).
- Amino Acid Content And Profile Of Some Proteinaceous Foods

Methionine has higher molecular weight than cysteine, therefore when one substitutes equal amounts of the other in a protein composition, it gives a false impression that there aren't more cysteine molecules in relation to methionine than previously.
- The In Vivo Sparing of Methionine by Cysteine in Sulfur Amino Acid Requirements in Animal Models and Adult Humans (!)

Therefore Georgi is neglecting the idea of moderation and balance: too much cancer is bad, but so can be too little.

 

[Amazoniac]

I just want to clarify that this has nothing to do with world travelers that are trying to escape themselves without realizing that kids make any environment interesting and learn from it.

Regarding our knowledgeable macrobe's position, I amn't disputing the fact that methionine restriction is beneficial. The matter here is how low it's desirable to go, what are the consequences of doing so and if there are conditions that call for more than the minimum.

The treshold for excess that he has in mind is a figure that's challenging to attain on a nourishing diet, and since it's impractical to go that low without compromising other aspects, this puts most people on excessive intakes and implies that there's virtually no low end if you're getting proper nutrition, therefore a person can cut it as desired without consequences, and perhaps accentuate this by taking the synthetic amino acids. This is a skin to iron and its tendency to accumulate, and viewing it as a target that always has to be lowered, and no matter how successful you is, there will be no negative effects from such measure.

I still don't know how common an actual methionine accumulation is outside of serious liver complications, the usual issue appears to be the elevation of homocysteine, which doesn't necessarily indicates excessive consumption; yet it does if you judge based on the competence to metabolize it. The less you consume, the less evident the problem will be.

I think that what's often missing from discussions is not what to do, but how to do properly. This is the challenging part that will make interventions sustainable and successful.


The average synthesis of taurine in wealthy people is claimed to be 50-125 mg/d (or less?), yet it's very common to respond favorably to more dietary taurine (it's almost the norm, especially in stressful conditions), which suggests sub and optimal synthesis.

For someone consuming a diet extremeky low in methionine, dietary taurine intake will be insignificant: it will have to be synthesized. Assuming that those values above are correct and that more is probably desirable, you have to be consuming enough sulfur in the diet for its proper synthesis because forcing the body to synthesize less is not a good idea.

If the methionine intake is at 140 mg/d (2 mg/kg bw), there's no way for this amount to provide enough sulfur to form 125 mg (or more) of taurine because once homocysteine is used for this purpose, it doesn't matter how much methyl groups you have available, there will be nothing for them to regenerate. In one of the articles posted they even suggested that cysteine can be helpful for those with elevated homocysteine because it indicates an impairment in this route and possibly not elsewhere, so when you provide cysteine, it will encourage methionine regeneration from homocysteine, making it useful again. This is related to its sparing effect.

It's one sulfur atom per methionine or taurine molecule. After adjustment based on what was commented on the previous post, if all of the 140 mg was adsorbed and used for taurine synthesis, it could synthesize no more than 110 mg of taurine, and this is disconsidering everything else.

So that can't happen and its sulfur has to come from diversified sources.

Adaptation to low intakes will occur, and perhaps experiments didn't wait long enough for this to happen, but how much of it is beneficial?
- Dietary Sulfur Amino Acid Restriction and the Integrated Stress Response: Mechanistic Insights

It's estimated that people obtain on average 1000 mg of sulfur per day just from methionid and cysteid. The 2 mg met/kg/d figure provides 0.5 mg S/kg/d, therefore 70 mg/d for example (cysteine intake could double it). There will be the intake of sulfate to spare it, but assuming that it remains unchanged, the sulfur intake is being dropped at least in half. This is a brutal difference and should be impactful when we consider the idea above that people tend to respond favorably to taurine or even cysteine.

- Is we getting enough sulfur in our diet? Yes, but this is interesting nevertheless:

Spoiler

- World map of protein consumption


However!

- Multiple sclesoris and other hormone-related brain syndromes

"Nutritional supplements that might help to prevent or correct these brain syndromes include: Vitamin E and coconut oil; vitamin A; magnesium, sodium; thyroid which includes T3; large amounts of animal protein, especially eggs; sulfur, such as magnesium sulfate or flowers of sulfur, but not to take continuously, because of sulfur's interference with copper absorption; pregnenolone; progesterone if needed."​

This is what I mean by not being able to separate these amino acids when consuming more protein. I'm not sure if excluding them would lead to better outcomes in those interventions on gurus dealing with liver issues (the thread linked before).


Lumping methionine and cysteine together makes it confusing. For example, when it's recommended 15 mg/kg/d, it can be an intake of 10 mg/kg of methionine and the rest from cysteine. In the cancre experiment on methionine restriction, it wased then 1.7 g of supplemental cysteine plus about 140 mg of dietary methionine and the same for cysteine (if they weren't consuming more from diet without realizing); but this amounts to 2 g of sulfur-containing amino acids a day, or 35 mg/kg/d. Looks like this in perspective:

Some values are just approximations.​

- Effect Of Taurine And N-acetylcysteine On Methionine Restriction-mediated Adiposity Resistance

Experiments used purified amino acids, so adsorption from foods must not be as high, this has to be accounted. But I do think it's possible to fare well on low intakes, however there are some caveats to it (as you can tell) and it must not be as low as 2 mg/kg/d.

 

[Amazoniac]

- A High-carb Diet May Explain Why Okinawans Live So Long

- 50 kg average body weight.
- 40 g of protein a day.

800 mg proteid/kg * 3% (as sulfur-containing amino acids): 24 mg/kg.​

 

[Amazoniac]

The title is not exciting, but the content is great:
- Sulfur metabolism and its contribution to malignancy (!)

 

[Amazoniac]

- Dysregulated Hepatic Methionine Metabolism Drives Homocysteine Elevation in Diet-Induced Nonalcoholic Fatty Liver Disease

↓​

- Resurgence of Serine: An Often Neglected but Indispensable Amino Acid (!)

 

[Amazoniac]

- Advanced Nutrition and Human Metabolism (978-1-133-10405-6)

Spoiler: Table 6.3: Some Enzymes Responsible for the Digestion of Protein

@BigYellowLemon

 

[Sativa]

Threonine is the one AA that I know relatively little about.

Apparently - L-Threonine is implicated in collagen production

 

[Elchapchapchapo]

Super grateful for this post, took 30gs of aminos yesterday and immeditely felt the effects, body become warmer, became very relaxed and sleep quality improved , i've slept 3 times since yesterday and it seems to be deeper, just grabbed glycine to add aswell to promote even deeper sleep.

Curious what exactly my body got from this but man I wish I just would of tried this earlier , i read this post a few times over the last couple years and i'm the type to try everything and i wish i would of tried this because i think that would of really healed me much sooner.

Thanks for sharing everyone

 

[NathanK]

Just catching up on this thread of yore....

How do we see Ray's article against amino acids here: Tryptophan, serotonin, and aging
"Beginning with the industrial production of glutamic acid (sold as MSG, monosodium glutamate), the public has been systematically misinformed about the effects of amino acids in the diet. The FDA has been industry's powerful ally in misleading the public. Despite research that clearly showed that adults assimilate whole proteins more effectively than free amino acids, much of the public has been led to believe that “predigested” hydrolized protein and manufactured free amino acids are more easily assimilated than real proteins, and that they are not toxic. Even if free amino acids could be produced industrially without introducing toxins and allergens, they wouldn't be appropriate for nutritional use.

Although some research shows that babies up to the age of 18 months can assimilate free amino acids, a baby formula containing hydrolyzed protein was associated with decreased serum albumin, which suggests that it interfered with protein synthesis.

My albumin and total protein increases with my version of this mix in my labwork. You bring up valid points, though

The atherogenic effect of excess methionine intake
"...Mice fed methionine-rich diets had significant atheromatous pathology in the aortic arch even with normal plasma homocysteine levels, whereas mice fed B vitamin-deficient diets developed severe hyperhomocysteinemia without any increase in vascular pathology. Our findings suggest that moderate increases in methionine intake are atherogenic in susceptible mice. Although homocysteine may contribute to the effect of methionine, high plasma homocysteine was not independently atherogenic in this model. Some product of excess methionine metabolism rather than high plasma homocysteine per se may underlie the association of homocysteine with vascular disease."

Excessive choline or TMAO precursors is also atherogenic. Gut Microbiota Metabolites and Risk of Major Adverse Cardiovascular Disease Events and Death: A Systematic Review and Meta-Analysis of Prospective ... - PubMed - NCBI

The safest way is to just eat eggs. Ideally, I try to get 2 soy free ones a day. Though, i did like your product :)

Thanks again. This thread has been important to me and my versions of this mix has helped me tremendously over the years. For one, it's exposed things in my labwork that I wouldn't have realized otherwise. Probably more people should look into this and not realize it.

@Amazoniac a follow up to some of the points you've been making to help round out your argument. I recall this was a follow up to the original study I posted
Taurine Blocks Methionine Absorption
"...taurine added to CDD caused decreased expression of PEMT,CHKa, and CHKb, key genes involved in phosphatidylcholine (PC) synthesis and liver fat accumulation."

 

[Amazoniac]

- Proteinogenic amino acid - Wikipedia

 

[Amazoniac]

- Plasma Amino Acid Concentrations After the Ingestion of Dairy and Collagen Proteins, in Healthy Active Males

Spoiler

"A number of AAs have been suggested to play a complementary role in the synthesis of collagen in ligaments and tendons, when combined with an appropriate mechanical stimulus (39). There is emerging evidence that the ingestion of key AAs (including proline, glycine, lysine, and leucine), or combinations thereof, provide enhanced availability to support the synthesis of collagen when combined with an appropriate exercise protocol (42)."

"It has been suggested that hydrolysis of collagen protein prior to ingestion allows two and three amino acid peptides to pass across the mucosal barrier equating to a higher expression and therefore biosynthesis within the tissue matrix (31). This was illustrated in a recent study whereby the consumption of hydrolysed collagen proteins resulted in a higher bioavailability of AAs compared to non-hydrolysed collagen protein and a placebo control (32). Furthermore, it has recently been shown that the consumption of collagen peptides resulted in a higher expression of collagen signaling proteins, compared to a placebo control (24)."

"Within the present study, the plasma characteristics of hydrolysed and nonhydrolysed dairy proteins showed some differences, but these were not seen with the collagen proteins."

Spoiler: Table 1. Details of proteins used (there's supplementary material)

Spoiler: Figure 1. Time course of plasma amino acid concentrations over 180 min after the consumption of collagen or dairy protein sources

"Data presented as mean ± SD."

Spoiler: Figure 2. Area under the concentration—time curve (AUC) of plasma amino acids over 180min after the consumption of dairy and collagen protein sources

"Middle line shows mean, boxes represent 25–75th percentile and whiskers represent min and max values."

"In general, plasma AA responses reflected the AA profiles of the consumed supplement, except in the case of the casein, and bone broth. These both resulted in a lower and more prolonged appearance of AAs in the blood over the 180 min following consumption (See Tables 1, 2 and Figure 2). This is likely due to various components known to slow gastric emptying such as the fat content of the BBr (43), and the clotting of casein in the stomach after ingestion (44). However, it is also plausible that the delayed gastric emptying of BBr may be related to the volume was consumed. As can be seen in Figure 1, the plasma concentration of AAs after consumption of BBr remained elevated at the 180 min mark, and most likely would have continued to be available at a higher amounts in the blood beyond the 3 h that were monitored for this study."

"It has been proposed that AAs play a supportive, rather than stimulatory role in the synthesis of collagen within ligaments and tendons (21, 39, 45). Meanwhile, exercise has been shown to be a potent regulator of collagen turnover resulting in an upregulation of collagen synthesis for a period of up to 72 h (46). Exercise results in an increase in hormones that have been shown to stimulate the synthesis of collagen in connective tissue (e.g., growth hormone, and insulin-like growth factor 1) (47)."

"As ligaments and tendons are poorly vascularised tissues, it may be sensible to isolate the provision of AAs to scenarios involving the exercise-induced enhancement of blood flow (48). Therefore, protein sources that achieve higher AA peaks over a shorter period of time (e.g., HCas) may be considered optimal, whereas a slower release of key AAs over an extended period of time (e.g., with BBr) may not be as easily matched to enhanced tissue blood flow."

"Literature to date suggests that there is dose related response to the key AA involved in the synthesis of collagen. Indeed, Shaw et al. (21) illustrated that a 15 g dose of gelatin resulted in an increased availability of AAs and collagen synthesis than a 5 g dose, resulting in improvements to tissue mechanics in engineered ligaments in vitro. Peak blood concentrations of glycine and proline in the current study (~650–750 and 350–450 µmol/L, respectively) were slightly higher than those reported in previous work [i.e., 448 ± 165 and 238 ± 77 µmol/L in Shaw et al. (21)]. This is to be expected given the slightly higher dose within our current protocol. However, others have shown similar plasma values after the ingestion of 35 g of collagenous protein (32) which they suggest shows an upper threshold to the AA availability of collagen proteins."

"Our findings are similar to the study of Koopman and co-workers where ingestion of 35 g of hydrolysed casein protein resulted in an increased bioavailability and incorporation rate of AAs into skeletal muscle protein than intact casein (50). However, while another more recent study showed that the ingestion of 35 g of enzymatically hydrolysed collagen resulted in a higher bioavailability of several AAs compared to non-enzymatically hydrolysed collagen (32), we did not find any difference in the bioavailability of gelatin compared to a hydrolysed peptide powder. It is possible that differences in processing methods accounted for this finding as it has been suggested to influence digestibility and therefore bioavailability of AAs (51)."

- Identification of Food-Derived Collagen Peptides in Human Blood after Oral Ingestion of Gelatin Hydrolysates

Spoiler

"In the present study, we isolated and identified some food-derived collagen peptides in human serum and plasma as shown in Table 2. Among them, Pro-Hyp, which has been demonstrated to be present in urine (15), is a major constituent in any case." "Healthy human volunteers ingested the gelatin hydrolysates (9.4-23 g) from porcine skin, chicken feet, and cartilage after 12 h of fasting." "In the case of the oral ingestion of chicken type II gelatin hydrolysates, a significant amount of Pro-Hyp-Gly was detected in human plasma. This motif is also abundantly present in type I and II collagens. However, only a lesser amount of Pro-Hyp- Gly was observed in the blood from those who ingested type I gelatin hydrolysates. The chicken type II gelatin hydrolysate preparation contained a significant amount of mucopolysaccharide (Table 1), which might affect digestion and absorption of collagen peptides. Another tripeptide, such as Gly-Pro-Hyp, could not be detected in all cases. Some dipeptides consisting of hydrophobic amino acids (Ile, Leu, and Phe) and Hyp are contained in human blood as minor constituents after loading of the gelatin hydrolysates. So far up to now, biological activities of them have not been described."

Spoiler

"[It has been demonstrated that] food-derived collagen peptides in human blood decreased to half of the maximum level after 4 h from the oral ingestion. In addition, more than 75% of Pro-Hyp remained after the in vitro reaction with human serum for 24 h. Therefore, Pro-Hyp can be considered as one of the indigestible peptides against peptidase in human blood. Pro-Hyp has been demonstrated to be excreted in urine without degradation (15). On the other hand, collagen peptides larger than Pro-Hyp-Gly could not be detected in all cases, while the gelatin hydrolysates used in the present study contained only negligible amounts of collagen peptides of less than 500 Da. These facts strongly suggest that the larger collagen peptides in the gelatin hydrolysates are degraded into tri- and dipeptides and free amino acids in the digestive tract and other organs."

"Recently, Koyama et al. reported that oral ingestion of gelatin can increase bone mineral density by an animal experiment (4)."

"Pro-Hyp has been also observed in the blood of patients suffering from bone metastases of prostatic cancer and osteoarthritis (24, 25). Then, Pro-Hyp in serum has been considered as a bone resorption marker. In addition, some in vitro studies demonstrated that Pro-Hyp and Pro-Hyp-Gly have chemotactic activity to human fibroblast and peripheral blood neutrophils and monocytes in the cell culture system (7-9). Migration of these cells has been demonstrated to play a critical role in the early stage of wound healing. These facts suggest that Pro-Hyp might act as a biological messenger of degradation of the extracellular matrix and trigger the wound healing process by stimulating migration of fibroblast and so on. In addition, collagen-derived oligo peptides have been demonstrated to show other biological activities, such as the inhibition of angiotensin-converting enzyme (11, 12), platelet activation (13), and so on."

 

[Amazoniac]

Wow is collagen and its glycine in spite of the other amino acids present? I couldn't find it posted, worth reading even if you have an evil amino acids category defined:

- Acquired Amino Acid Deficiencies: A Focus on Arginine and Glutamine (!)

 

[Amazoniac]

Bone dissolution or pre-digested collagen (sharper appearance of amino acids in spite of similar overall uptake?) ⭢ hydroxyprolide ⭢ oxalate (pg. 10/23)⭢ petrification ⭢ ER ⭢ resuscitation ⭢ discharge/home ⭢ excess collagen intake ⭢ low-tryptophan diet ⭢ niacin reliance ⭢ no intake ⭢ diarrhea ⭢ dermatitis ⭢ dementia ⭢ ER ⭢ resuscitation ⭢ home again but with hospital-acquired infection ⭢ more dietary collagen ⭢ no counteraction ⭢ extinguished nitrogen specie.

--
- Small Changes Huge Impact: The Role of Protein Posttranslational Modifications in Cellular Homeostasis and Disease

 

[Amazoniac]

- Branched-chain amino acids in health and disease: metabolism, alterations in blood plasma, and as supplements

"BCAAs are recommended to ameliorate cachexia and the decreased ratio of BCAAs to AAAs, which plays a role in the pathogenesis of hepatic encephalopathy. Potential benefits also include positive effects of the BCAA on ammonia detoxification to GLN in muscles, liver regeneration, albumin synthesis, immune and hepatic function, glucose metabolism, and physical and mental fatigue [20, 47–49].

Unfortunately, the results from clinical trials do not provide strong evidence of their beneficial effects [50, 51] and adverse effects of BCAA supplementation, which may compete with their benefits, have also been suggested [52]. The positive effects of BCAAs in subjects with liver cirrhosis may be blunted by enhanced catabolism of GLN produced in muscles to ammonia in visceral tissues, especially in the gut and kidneys. The draining of α-KG from TCA cycle may also be detrimental (Fig. 5). Therefore, therapeutic strategies are needed to avoid potential adverse effects of BCAAs on ammonia production and cataplerosis. Options include substitution of α-KG, glutamate related substrates (e.g. L-ornithine-L-aspartate), GLN elimination from the body by phenylbutyrate, replacement of BCAAs by BCKAs, and optimizing dose, proportions, and timing of BCAA supplementation [52]."​

 

[chanlaw]

These amino acids without the bad amino acids are way too expensive. crazy amount, around 300 for 100g worth of protein from it.

 

[tankasnowgod]

I've been supplementing some of the Amino Acids again, and came back to this thread of yore, as NathanK called it. I've been digging deep, and read the MAP diet that Haidut linked in the original post.

https://naturalsolutions.nz/articles/MAP-as-dietary-protein-substitute-for-weight-loss-Oct2003.pdf

It's pretty incredible. If you haven't seen the experimental diet, here it is-

Wow! So, that's like a full on Volumetrics approach, fruit and veg wise. Still, at around 6+ pounds of fruit a day, it's around 1,000-1,200 calories or so, which is a level some aim for when "crash dieting" in a PMSF way. Even though the Amino Acids are at 30g, they count basically nothing to calories, as the paper listed the full 30g at only 2 total calories. I guess they don't have the same caloric content as Protein, not even close.

The results of this diet are pretty incredible, too. An average of 5.3 pounds lost a week, while some people some weeks got up to 16 pounds of weight loss. They say lean tissue is preserved. The weight loss is fat and "excessive water retention from the interstitial compartment." Both sound like good things to me. The less water in the intestinal cabinet of Dr. Caligari, the better. (Yeah, the interstitial compartment is all over, and not just in the intestines, but I can't get that Caligari thing out of my head) Apparently, another paper showed a weight loss of about 3 pounds a week just doing 1 daily meal intervention like this instead of all three.

If you read through the paper, the subjects seem to have a number of good effects, and the longer term follow up showed them keeping the weight off, or even losing a bit more. Lot's of things to like in this diet (even with the bad aminos in MAP), like the lack of starch, lack of PUFA, and really all fat, and likely lead to reductions in FFA, endotoxin, ammonia, and improved liver function.

The one Pre-Peat dietary intervention that I loved, then hated, but still have fond memories of, is Intermittent Fasting. I'm starting to think the Modified MAP formula with fruit/juice/other pure sugars might be a good occasional substitute. I loved IF as a weight melting tool, and it was great Pre/Post binge meals too. It certainly seemed to have a cleansing aspect, too. I tried Modified MAP plus juice or fruit for Breakfast and Lunch..... and I hit sort of the "clean running clarity" that I remember from the good IF days. Maybe less FFA, maybe less ammonia, maybe just good to have less food in the intestinal cabinet for a bit, maybe gave the liver a chance to process a backlog.

Certainly gonna try this again, although I'm not gonna go super nuts with this like I did when I was doing IF. But it's great that I might have finally found a tool that can replace that, without doing damage to metabolism or muscle.

 

[Amazoniac]

I've been supplementing some of the Amino Acids again, and came back to this thread of yore, as NathanK called it. I've been digging deep, and read the MAP diet that Haidut linked in the original post.

https://naturalsolutions.nz/articles/MAP-as-dietary-protein-substitute-for-weight-loss-Oct2003.pdf

It's pretty incredible. If you haven't seen the experimental diet, here it is-

View attachment 20142

Wow! So, that's like a full on Volumetrics approach, fruit and veg wise. Still, at around 6+ pounds of fruit a day, it's around 1,000-1,200 calories or so, which is a level some aim for when "crash dieting" in a PMSF way. Even though the Amino Acids are at 30g, they count basically nothing to calories, as the paper listed the full 30g at only 2 total calories. I guess they don't have the same caloric content as Protein, not even close.

The results of this diet are pretty incredible, too. An average of 5.3 pounds lost a week, while some people some weeks got up to 16 pounds of weight loss. They say lean tissue is preserved. The weight loss is fat and "excessive water retention from the interstitial compartment." Both sound like good things to me. The less water in the intestinal cabinet of Dr. Caligari, the better. (Yeah, the interstitial compartment is all over, and not just in the intestines, but I can't get that Caligari thing out of my head) Apparently, another paper showed a weight loss of about 3 pounds a week just doing 1 daily meal intervention like this instead of all three.

If you read through the paper, the subjects seem to have a number of good effects, and the longer term follow up showed them keeping the weight off, or even losing a bit more. Lot's of things to like in this diet (even with the bad aminos in MAP), like the lack of starch, lack of PUFA, and really all fat, and likely lead to reductions in FFA, endotoxin, ammonia, and improved liver function.

The one Pre-Peat dietary intervention that I loved, then hated, but still have fond memories of, is Intermittent Fasting. I'm starting to think the Modified MAP formula with fruit/juice/other pure sugars might be a good occasional substitute. I loved IF as a weight melting tool, and it was great Pre/Post binge meals too. It certainly seemed to have a cleansing aspect, too. I tried Modified MAP plus juice or fruit for Breakfast and Lunch..... and I hit sort of the "clean running clarity" that I remember from the good IF days. Maybe less FFA, maybe less ammonia, maybe just good to have less food in the intestinal cabinet for a bit, maybe gave the liver a chance to process a backlog.

Certainly gonna try this again, although I'm not gonna go super nuts with this like I did when I was doing IF. But it's great that I might have finally found a tool that can replace that, without doing damage to metabolism or muscle.

Purified amino acids will likely induce micronutrient deficiencies, every meal had a tablet of 'VIT-formula'. Digesting protein takes longer (peptides compared to proteids), it's an opportunity for the body to make adjustments and reallocate nutrients according to what's available, perhaps measures that retard release from the stomach may be of welp. And this is considering that they're consumed in the right proportions, or else it's one additional disturbance.

You'd have to watchout for quality as well, it's tens of grams of synthetic material. Most of our concern in this regard is with compounds that are not consumed in doses greater than 5 g (killcium, laxarium, creatine*, and so on), only sea salt may get that high, yet Mother Nature can't do harm.

*Officializing here that this term will no longer exist in Prolactinese, from now on 'crematine' should be adopted. It's not that the speaker who uses terms from obsolete languages is going to be expelled from the society as it may happen with impurities being excluded when large salt crystals are formed, it is fine like the dirty salt scrapes, but discouraged.

 

[Sven90]

I've been supplementing some of the Amino Acids again, and came back to this thread of yore, as NathanK called it. I've been digging deep, and read the MAP diet that Haidut linked in the original post.

https://naturalsolutions.nz/articles/MAP-as-dietary-protein-substitute-for-weight-loss-Oct2003.pdf

It's pretty incredible. If you haven't seen the experimental diet, here it is-

View attachment 20142

Wow! So, that's like a full on Volumetrics approach, fruit and veg wise. Still, at around 6+ pounds of fruit a day, it's around 1,000-1,200 calories or so, which is a level some aim for when "crash dieting" in a PMSF way. Even though the Amino Acids are at 30g, they count basically nothing to calories, as the paper listed the full 30g at only 2 total calories. I guess they don't have the same caloric content as Protein, not even close.

The results of this diet are pretty incredible, too. An average of 5.3 pounds lost a week, while some people some weeks got up to 16 pounds of weight loss. They say lean tissue is preserved. The weight loss is fat and "excessive water retention from the interstitial compartment." Both sound like good things to me. The less water in the intestinal cabinet of Dr. Caligari, the better. (Yeah, the interstitial compartment is all over, and not just in the intestines, but I can't get that Caligari thing out of my head) Apparently, another paper showed a weight loss of about 3 pounds a week just doing 1 daily meal intervention like this instead of all three.

If you read through the paper, the subjects seem to have a number of good effects, and the longer term follow up showed them keeping the weight off, or even losing a bit more. Lot's of things to like in this diet (even with the bad aminos in MAP), like the lack of starch, lack of PUFA, and really all fat, and likely lead to reductions in FFA, endotoxin, ammonia, and improved liver function.

The one Pre-Peat dietary intervention that I loved, then hated, but still have fond memories of, is Intermittent Fasting. I'm starting to think the Modified MAP formula with fruit/juice/other pure sugars might be a good occasional substitute. I loved IF as a weight melting tool, and it was great Pre/Post binge meals too. It certainly seemed to have a cleansing aspect, too. I tried Modified MAP plus juice or fruit for Breakfast and Lunch..... and I hit sort of the "clean running clarity" that I remember from the good IF days. Maybe less FFA, maybe less ammonia, maybe just good to have less food in the intestinal cabinet for a bit, maybe gave the liver a chance to process a backlog.

Certainly gonna try this again, although I'm not gonna go super nuts with this like I did when I was doing IF. But it's great that I might have finally found a tool that can replace that, without doing damage to metabolism or muscle.

Sometimes I follow this kind of approach if I had too much food the day before. But to be honest I could not eat "only" fruit for several days. I would be hungry as hell. Zero or low fat = Hunger