Dr. William Frederich Koch USA/Brazil, Drs. Erich & Dieter Reinstorff, Germany - Discussion Thread

[Travis]

So would supplementing lysine probably not be a good idea?

The diamine cadaverine is formed from the decarboxylation of lysine, and the diamine putrescine is formed upon decarboxylation of ornithine—formed from either methionine or arginine. It has been shown in the rat that ornithine decarboxylase—the main polyamine producing enzyme—is also responsible for the decarboxylation of lysine.*

Lysine decarboxylase activity executed by ornithine decarboxylase.

'The present experiments indicate that rat tissues do contain a lysine decarboxylase activity capable of producing cadaverine, but indicate that all of this activity is due to the action of ornithine decarboxylase.' ―Pegg

'Persson [15] has also concluded that mouse kidney ornithine decarboxylase acts on lysine.' ―Pegg

'The present experiments are in agreement with those of Bey et al. [37] in indicating that the active center for omithine decarboxylase strongly prefers the distance between the amino groups to be that of four carbon atoms. However, it is shown here five carbons can be accommodated with a reduced affinity.' ―Pegg

'But this lysine decarboxylase activity by ornithine decarboxylase, to form cadaverine, is less specific and slower than the decarboxylation of ornithine to produce putrescine. Lysine is less of a substrate, and much less cadaverine is produced in tissues.' ―Pegg

'For this reason, although the V with lysine was about 25% that with ornithine (Table V), the degree of lysine decarboxylation is likely to be small in most tissues' ―Pegg​

click to embiggen​

'However, it remains possible that in tissues other than liver which has a relatively high ornithine content, there might be significant decarboxylation of lysine to form cadaverine. In particular, the possibility that cells in culture which may be exposed to substantially higher concentrations of lysine than ornithine may produce cadaverine as well as putrescine appears to be worthy of consideration.' ―Pegg​

Methionine and arginine seem of more concern, as they both form ornithine—the substrate of higher affinity. But since arginine can be disabled by methylgloxal (imidazalone formation), this amino acid could be less of a factor. (Arginine is also responsible for the body's nitric oxide.) Most researchers seem to agree that excess methionine determines polyamine synthesis more than any other amino acid.

Polyamines increase growth, and may be desired—by some—for this reason. But if a person wants a reduction in size and growth, a reduction in these aforementioned amino acids may be a good idea. If someone has cancer, the amino acid threonine would probably be the one to consume—certainly not methionine. Threonine is a precursor to methylglyoxal.

I think part of the reason why Gerson and Koch give people fruit is because it is lower in total protein than most foods, and also has a lower ratio of methionine over the total protein (and has vitamins!). Once a tumor has formed, I think it's fair to assume that it has a higher ornithine decarboxylase activity than most tissues;† tumors have been shown to turn excessive methionine into polyamines at a relatively quick rate. In cancer, it could be a good to have arginine and methione as the limiting amino acids. This can probably be accomplished by consuming fruit, leaves, and gelatine—essentially the same dietary strategy found effective by Gerson and Koch. (But Charlotte Gerson is deluding herself with linoleic acid recommendations; either that, or she's getting paid to discredit her own Dad's research (facetious). Linoleic acid is one of the main risk factors in prostate cancer; it probably does this by first becoming leukotriene B4, which then goes on the upregulate the enzyme ornithine decarboxylase (of all things).).‡

[*] Pegg, Anthony E. "Decarboxylation of ornithine and lysine in rat tissues." Biochimica et Biophysica Acta (BBA)-Enzymology (1979)
[†] O'Brien, Thomas. "Ornithine decarboxylase overexpression is a sufficient condition for tumor promotion in mouse skin." Cancer Research (1997)
[‡] Belury, Martha A. "Dietary conjugated linoleic acid induces peroxisome-specific enzyme accumulation and ornithine decarboxylase activity in mouse liver." The Journal of nutritional biochemistry (1997)​

 

[Amazoniac]

gelatine

Travisord, I doubt it would work as it's really complementary to muscle meat, unless very little is consumed. Remember this thread?
Gelatin Can Exarcerbate A Protein Insufficiency

 

[Travis]

Travisord, I doubt it would work as it's really complementary to muscle meat, unless very little is consumed. Remember this thread?
Gelatin Can Exarcerbate A Protein Insufficiency

Good point. I just thought that I had to mention a Peat‐oriented food once in a while, so that I don't get lynched by the Peat‐mob.

Gelatin doesn't have many amino acids, but the ones that it does have—such a glycine and proline—are not polyamine precursors; but gelatin can lead to unnatural amino acid ratios since it's basically just hydrolyzed collagenaceous remnants of cow bones left‐over from the beef and leather industries.

But then again: Is amino acid imbalance conducive to cancer? Could small additional amounts of hydroxyproline increase collagen synthesis without forming polyamines? or perhaps divert excessive methione, lysine, and arginine towards new protein synthesis? —removing them from the free amino acid pool and dashing their aspirations to become polyamines?

Not sure, but it might be worth looking in to. Fruit appears to have a cancerostatic amino acid profile as it is, but perhaps small amounts of gelatin could be beneficial—but then again: maybe not. Perhaps instead of gelatin, it would simply be better to consume more fruit (or keep the gelatin under about seven grams).

 

[Amazoniac]

Perhaps instead of gelatin, it would simply be better to consume more fruit.

I was expecting this sentence finishing with isolated amino acids such as glycine, but fruit should work too.
I have some doubts about threonine as well. I know in theory it looks very good, but in practice I don't know if proteins or peptides facilitate amino acids' absorption when combined; or if it would create some other imbalance; or serve as food for bacteria, just like undigested glutamic acid from collagen.

l-Glutamine regulates amino acid utilization by intestinal bacteria

A Deficiency or Excess of Dietary Threonine Reduces Protein Synthesis in Jejunum and Skeletal Muscle of Young Pigs
The anaerobic degradation of l-serine and l-threonine in enterobacteria: networks of pathways and regulatory signals​

It's difficult to make single nutrients work on a debilitated person because there's already difficulty in finding balance even when the diet is of excellent composition, Ray's "In the presence of hypothyroidism and magnesium deficiency everything is dangerous". Isolated amino acids are always tricky, but perhaps I'm missing something.

Another point against gelatin is that it might require the muscle protein stimulus for proper digestion of its complex parts, especially when the person is compromised.

 

[charlie]

The diamine cadaverine is formed from the decarboxylation of lysine, and the diamine putrescine is formed upon decarboxylation of ornithine—formed from either methionine or arginine. It has been shown in the rat that ornithine decarboxylase—the main polyamine producing enzyme—is also responsible for the decarboxylation of lysine.*

Lysine decarboxylase activity executed by ornithine decarboxylase.

'The present experiments indicate that rat tissues do contain a lysine decarboxylase activity capable of producing cadaverine, but indicate that all of this activity is due to the action of ornithine decarboxylase.' ―Pegg

'Persson [15] has also concluded that mouse kidney ornithine decarboxylase acts on lysine.' ―Pegg

'The present experiments are in agreement with those of Bey et al. [37] in indicating that the active center for omithine decarboxylase strongly prefers the distance between the amino groups to be that of four carbon atoms. However, it is shown here five carbons can be accommodated with a reduced affinity.' ―Pegg

'But this lysine decarboxylase activity by ornithine decarboxylase, to form cadaverine, is less specific and slower than the decarboxylation of ornithine to produce putrescine. Lysine is less of a substrate, and much less cadaverine is produced in tissues.' ―Pegg

'For this reason, although the V with lysine was about 25% that with ornithine (Table V), the degree of lysine decarboxylation is likely to be small in most tissues' ―Pegg​

View attachment 7621 View attachment 7622 click to embiggen​

'However, it remains possible that in tissues other than liver which has a relatively high ornithine content, there might be significant decarboxylation of lysine to form cadaverine. In particular, the possibility that cells in culture which may be exposed to substantially higher concentrations of lysine than ornithine may produce cadaverine as well as putrescine appears to be worthy of consideration.' ―Pegg​

Methionine and arginine seem of more concern, as they both form ornithine—the substrate of higher affinity. But since arginine can be disabled by methylgloxal (imidazalone formation), this amino acid could be less of a factor. (Arginine is also responsible for the body's nitric oxide.) Most researchers seem to agree that excess methionine determines polyamine synthesis more than any other amino acid.

Polyamines increase growth, and may be desired—by some—for this reason. But if a person wants a reduction in size and growth, a reduction in these aforementioned amino acids may be a good idea. If someone has cancer, the amino acid threonine would probably be the one to consume—certainly not methionine. Threonine is a precursor to methylglyoxal.

I think part of the reason why Gerson and Koch give people fruit is because it is lower in total protein than most foods, and also has a lower ratio of methionine over the total protein (and has vitamins!). Once a tumor has formed, I think it's fair to assume that it has a higher ornithine decarboxylase activity than most tissues;† tumors have been shown to turn excessive methionine into polyamines at a relatively quick rate. In cancer, it could be a good to have arginine and methione as the limiting amino acids. This can probably be accomplished by consuming fruit, leaves, and gelatine—essentially the same dietary strategy found effective by Gerson and Koch. (But Charlotte Gerson is deluding herself with linoleic acid recommendations; either that, or she's getting paid to discredit her own Dad's research (facetious). Linoleic acid is one of the main risk factors in prostate cancer; it probably does this by first becoming leukotriene B4, which then goes on the upregulate the enzyme ornithine decarboxylase (of all things).).‡

[*] Pegg, Anthony E. "Decarboxylation of ornithine and lysine in rat tissues." Biochimica et Biophysica Acta (BBA)-Enzymology (1979)
[†] O'Brien, Thomas. "Ornithine decarboxylase overexpression is a sufficient condition for tumor promotion in mouse skin." Cancer Research (1997)
[‡] Belury, Martha A. "Dietary conjugated linoleic acid induces peroxisome-specific enzyme accumulation and ornithine decarboxylase activity in mouse liver." The Journal of nutritional biochemistry (1997)​

I appreciate your detailed reply, thank you. Now off to down some B1 and coffee so I can fully comprehend it.

 

[Travis]

I appreciate your detailed reply, thank you. Now off to down some B1 and coffee so I can fully comprehend it.

My chemdraw software licence has unfortunately expired, so I can no longer draw the illustrations. Polyamines make more sense when you can just look at the amino acid structure, watch it become decarboxylated, and then see the resultant polyamine. It's good to know that lysine isn't much of a substrate for polyamine synthesis, so methione is the one to be most to be most concerned about (it forms homocysteine too). I don't see anyone taking methionine, and it wouldn't surprise me if it was actually illegal (researchers barely escape animal abuse charges after giving it to rats).

 

[Such_Saturation]

My chemdraw software licence has unfortunately expired, so I can no longer draw the illustrations. Polyamines make more sense when you can just look amino acid structure, watch it become decarboxylated, and then see the resultant polyamine. It's good to know that lysine isn't much of a substrate for polyamine synthesis, so methione is the one to be most to be most concerned about (it forms homocysteine too). I don't see anyone taking methionine, and it wouldn't surprise me if it was actually illegal (researchers barely escape animal abuse charges after giving it to rats).

Which software did you use?

 

[Travis]

Which software did you use?

I use . . . ChemDoodle version 8.0. I like this because you can make bonds of varying thickness; specifically: the wedge‐bonds—that project above the plane of the page—can be made less prominent. I like to see wedge‐bonds a bit thinner, less gaudy, and think standard chemical line drawings can continue to be improved slightly (no doubt there's some old man out there, somewhere, who still draws indole like this). I did find this free program called Avogadro, which can allow one to reconstruct whole proteins. This will not make line depictions, because it's better, but will create geometrically‐accurate ball‐and‐stick models. I typed‐in the eight amino acid repeat of α-gliadin, a peptide which is mostly proline and glutamine (QPQPFPQQPYP), as an example. I chose this peptide since it powerfully induces interferon-γ in some people, reduces intestinal crypt length, increases prostaglandins (arthritis; asthma), and can induce a that veritable histaminergic brain damage that some call autism and others call schizophrenia (depending on age).

Here are a few different views:

click to embiggen

There are other projections, or flavors, but I like these ones here. The image on the right has an additional ring-filling layer with pastel colors (no choice, it wasn't me. It was . . . them!) giving it a unique look, almost reminiscent of those cellophane-dipped wires bent in the shape of flowers.

This is an open source program, and I think if you had enough memory on your computer you could create an entire microtubule. This program calculates energies, but I don't know if I'd trust it 100% to recreate a β-tubulin from the amino acid sequence. It couldn't hurt to try, and then compare the resulting image with a published one and inspect it manually (keeping in mind things like the hydrophobic effect and the Ramachandran plot). I could take some manipulation to add one tubulin monomer to another, but I think it could be done. It would be nice to have some better images of the insides of microtubules—with particular emphasis on the fluorescent indoles, phenyls, phenols, and imidazoles of the amino acids tryptophan, phenylalanine, tyrosine, and histidine (viewed in the wire frame pastel, psychedelic, plastic-dipped projection of course).

 

[Cliff Myles]

One possibility might be for an MD to administer pure water into the muscle, and then immediately thereafter also inject the SSR or mixed glyoxal/meglyoxal into the same area. This would provide the ruptured cell contents to be present from the cell walls' rupturing, and also the active dehydrogenators.

Actually, the much preferred method that Koch insisted on was IV intravenous direct delivery. In a syringe, (ideally) the reagent is first drawn through a non-metallic needle, then a large stainless needle is affixed and inserted into a vein, an equal amount of blood is drawn in with the reagent, then slowly pushed in slowly over a one-minute period.

 

[Travis]

The physical effects of polyamines on DNA seem to be limited to the transition to the Z-configiration by spermine. Other polyamines—such as the diamines putrescine and cadaverine—have no real effect, yet serve as direct precursors to spermine. The Z-configiration of DNA is radically different that the common Watson–Crick B-configiration, and is characterized by a helix of opposite twist. This drastic transitional charge is likely how spermine executes its catalytic role in DNA synthesis velocity, and also why the generative enzyme ornithine decarboxylase is so correlated with cell states characterized by accelerated proliferation.

The idiosyncratic effect that polyamines excert on DNA had been observed since the early '60s; so peculiar was the interaction that it had been observed less than a decade after it's structure had been elucidated. The early studies had noticed changes in viscosity, melting temperature, and UV absorbance.

'While their specific biological functions are not known, polyamines and diamines have been shown to interact with DNA and bring about an increased resistance to temperature induced unfolding (Mahler and Mehrotra, 1962; Mandel, 1962; Tabor, 1962). This increase in "melting" temperature has been correlated with adenine-thymine content of the DNA.' ―Kaesberg (1963)​

From such measurements a primitive idea was born, one that still persists: The phrase 'polyamines stabilize DNA' is a common, as can be verified with a simple Google search. It is difficult to maintain this meme while also observing the experimental data indicating that polyamines act to replicate; the two thoughts that polyamines both stabilize, and uncoil, is hard to reconcile. What they seem to accomplish is a destabilization of the B-configiration, the creation of a Z-configiration, and an increase DNA synthesis.

https://upload.wikimedia.org/wikipedia/commons/b/b9/A-B-Z-DNA_Side_View.png

[The A-configuration, the B-configuration, and the Z-configuration listed alphabetically from left to right.]

This has been conclusively shown through circular dichoism studies. Molecules with chirality, and especially large helical ones, are known to rotate plane-polarized light. This makes circular dichroism the perfect choice for investigating a right-handed to left-handed helical twist inversion. When this is done, it is found that the diamine putrescine does nothing: it's too small, and not literally even a polyamine. Spermidine—essentially two putrescine molecules fused together—does better, but the trimer spermine works far better than all the rest.

click to embiggen: Changes in circular dichroism with graded concentrations of spermine (left) of spermidine (right).

These changes can also been seen by gel electrophoresis, as the Z-configuration is stiffer and cannot migrate as far against increasing gel density.

click to embiggen: Changes in electrophoretic gel migration with spermine-induced DNA helical inversion.

Polyamine-starved cells will not replicate, highlighting their essential role in cell division. Also illustrating their importance is the fact that sperm consists of very high levels of spermine, which ostensibly replicates the first cell (ova) of a new organism. For this reason the prostate produces more polyamines than any other; prostate cancer is also the number one cancer in the West.

'The data presented in Table 1 show a remarkable chemical structural effect of polyamines in provoking the Z-DNA conformation of poly(dGm⁵dC). poly(dG-m⁵dC).' —Thomas​

In Poland, in 1996, twelve different polyamines were study as catalysts in a polymerase chain reaction (PCR). Spermine was found to catalyze the rate of DNA synthesis; the others were mostly without effect:

click to embiggen: Northern blot showing DNA amplification in lanes 9–11.

Since spermine induces the Z-configuration, and spermine increases DNA synthesis rates, you are forced to assume that the Z-configuration increases DNA synthesis rates. Notable is that 'methylation islands,' or CpG repeats, have a lower energetic barrier towards the Z-configuration; you might expect areas of high cytosine‐5‐methylation to replicate faster, or serve as a region of initiation, as they should be found in the Z-configuration at relatively low spermine concentrations—concentrations in which other regions are still in B-configuration.

Soy sauce is unusually high in polyamines. The Japanese have high rates of stomach cancer.

'Among a series of trivalent aliphatic triamines. spermidine is the most efficient inducer of the transition. The structural effect of spermidine homologs in B-DNA to Z-DNA transition is comparable with the regulatory effects of these compounds in cell growth.' —Thomas​

Modeling has been done. Since the Z-configuration is characterized by a backbone inversion, it's logical to assume that spermine spans the phosphate groups on the backbone—having their positively‐charged amines attracted to, and binding with, the negatively‐charged phosphate oxygens:

click to embiggen: Image depicting spermine bound to DNA backbone.

[Amin Ahmed Ouameur didn't get the memo, and is using an image of DNA in the B-configuration.]

The experimental data greatly simplifies the important DNA–polyamine interactions, as spermine, and to a much lesser degree spermidine, are the only two polyamines really worth considering. The smaller ones, such as putrescine and cadaverine, seem important only to the extent that they condense to form the larger ones.

Paul Kaesberg. "Interaction of polyamines with turnip yellow mosaic virus RNA." Biochemical and Biophysical Research Communications (1963)
Fiedorow, Paweł. "The influence of polyamines on polymerase chain reaction (PCR)." ACTA BIOCHIMICA POLONICA-ENGLISH EDITION (1997)
Thomas, T. J. "Structural specificity of polyamines in left-handed Z-DNA formation: immunological and spectroscopic studies." Journal of molecular biology (1988)
Parkinson, Andrew. "Amine induced Z-DNA in poly (dG-dC)· poly (dG-dC): Circular dichroism and gel electrophoresis study." Physical Chemistry Chemical Physics (2000)
Ouameur, Amin Ahmed. "Structural analysis of DNA interactions with biogenic polyamines and cobalt (III) hexamine studied by Fourier transform infrared and capillary electrophoresis." Journal of Biological Chemistry (2004)
​

 

[Amazoniac]

The sulfur-containing amino acids are known for causing trouble in susceptible people, in cancer they should be enough to halt the guru's progress (below).
Taurine, methionine, cysteine (even NAC has flatulence as a common initial side-effect).

Sulfur as a Signaling Nutrient Through Hydrogen Sulfide

Here's the entire paragraph that touches on hydrogen sulfide.
http://www.williamfkoch.com/web/version2/drkoch.php?id=30.0&dispID=disp(1);
"This brings us down to the Carbonyl catalysts which we credit with serving the tissue oxidations for work energy production, and which arise in the oxidation of sugar. The Carbonyl group is always more or less of a hydrogen acceptor, but when it is especially activated as by conjugation with ethylene or acetylene or in series with other Carbonyl groups, it is then that this activity is most pronounced and useful. The most active of such arrangements are, of course, the union of two Carbonyl groups with double bonds. But this is a special subject. The protection of Carbonyl in conjugation with ethylene must again take into consideration the sulfydryl group as present in hydrogen sulfide particularly, and so the use of animal proteins of all types comes up as an offense against good recovery chemistry. A patient may “get by” while eating animal proteins. In fact, the stuffing of patients with animal proteins in hospitals to “give them strength” as they say can be credited with many failures in the ordinary infections like pneumonia and tuberculosis. In cancer it is simply fatal and rapidly so in the whole field of observations that we have made. We have recommended bone broth for its calcium content in the past, and it has been used safely in some patients. But we soon learned that all patients could not take even this, and we saw too many develop indole and skatol in the urine after its use. We therefore discontinued this effort to supply useful food materials in a way that satisfies the cravings for meat of a good part of our patients. Not only are the metallic catalysts endangered by the sulfides, but additions are made to Carbonyl-ethylene conjugates which inactivate them. They also liberate highly active hydrogen that makes additions to free radical oxidation carriers. Of course, when Nature has her most important tools rendered useless in this way, she supplied her second line of agents to do what they can to keep the system going, but this is not what we want. To combat serious disease we must have the best that Nature can offer, and indeed we must add to this even more active oxidation agents than Nature regularly uses, so far as we know. It is to supply such Carbonyl compounds that we have built up our initiators of oxidation chains as we have. But since they are more active than any we know in Nature, they are all the more reactable with the sulfide and amine or the aromatic inhibitors produced by meat putrefaction within the intestinal tract. Thus the pure vegetarian, fruit diet is all the more necessary, while our Treatment is used."

"The dog is essentially carnivorous with a protein digestive capacity of high caliber. They may masticate or swallow the meat chunks whole and thrive nutritionally. Yet they often die of cancer. On a pure meat diet, however, they form fewer sulfides than on a mixed diet."
Interesting.

 

[Travis]

Methione is a thiol but is actually converted into ornithine, then into polyamines. There is a technical word for this called . . . doubleplusbad.

 

[Amazoniac]

Methione is a thiol but is actually converted into ornithine, then into polyamines. There is a technical word for this called . . . doubleplusbad.

It's difficult to question when you pull a Orentreich but there are examples showing that some is desirable:
Long-lived Compilation Facts
Fish appears more often than chicken which appears more often than red meat, which is what we would've expected.

 

[Travis]

It's difficult to question when you pull a Orentreich but there are examples showing that some is desirable:

Desirable? why?

Is it because: When you prostate explodes from all the excessive polyamines, the excessive homocysteine makes you too demented to care?

 

[Amazoniac]

Desirable? why?

Is it because: When you prostate explodes from all the excessive polyamines, the excessive homocysteine makes you too demented to care?

I doubt they would've lived longer and better if they restricted methionine (more?). Out of labs things can be more complicated, here's an example:
Seasoning, Spices And Preservatives Protect Your Food From Microbes (even After Ingestion)
__
What's the reason for a smaller font?

 

[Amazoniac]

@burtlancast - Do you have his other books that are not available on the family's website?

 

[Travis]

I doubt they would've lived longer and better if they restricted methionine (more?). Out of labs things can be more complicated, here's an example:
Seasoning, Spices And Preservatives Protect Your Food From Microbes (even After Ingestion)
__
What's the reason for a smaller font?

Well of course we need polyamines, as the cell will actually die without them ('polyamine starvation' is a scientific concept). However: the relatively low activity polyamine derived from lysine (at center) can still sustain the cell, albeit without the high proliferative capacity of spermine and spermidine. We can also of course make ornithine from arginine, but arginine is an ṄO hazard (the N-dot means free radical electron; this I'll always make explicit lest someone actually forget—and also out of formalistic pedantry—that nitric oxide is a free radical, this being the inherent property underlying its danger). But it can also not be argued that a very small increase in methionine causes phenyotypical changes of greater magnitude than the like supplementation of any other amino acid. The feeding of a slight excess of tryptophan only caused a reduction in lifespan of 13%, most likely the result of brain serotonin increasing growth hormone. But as brain serotonin is dependent on Fernstromian pharmacokinetics, the ratio likely means more than the absolute amount—and something not liable to get too unbalanced lest one live primarily on lean meat (or is crazy enough to take L-tryptophan supplements). But even then, most anyone with slight immune activation having circulating interferon-γ would be expected to degrade a good amount of any excess tryptophan through the kynurenine pathway, this always induced by the foregoing cytokine through indolamine and tryptophan diooxygenases. I really think methionine can rightly be considered a growth factor: Methionine had caused the rats to balloon and had reduced their lifespans by over a third—and two separate studies by separate and unrelated researchers. I don't think anyone in America has to worry about having 'too little polyamines,' but I still do maintain that many should be concerned about eating too much methionine.

 

[burtlancast]

@burtlancast - Do you have his other books that are not available on the family's website?

I've mentioned here that his first book, "Cancer and its allied diseases; their common toxic cause, their cure by immunization" is only available in natioanal libraries, mostly from USA, and i don't have it.

I believe that's the only work his family website doesn't have available for download.

 

[Amazoniac]

Well of course we need polyamines, as the cell will actually die without them ('polyamine starvation' is a scientific concept). However: the relatively low activity polyamine derived from lysine (at center) can still sustain the cell, albeit without the high proliferative capacity of spermine and spermidine. We can also of course make ornithine from arginine, but arginine is an ṄO hazard (the N-dot means free radical electron; this I'll always make explicit lest someone actually forget—and also out of formalistic pedantry—that nitric oxide is a free radical, this being the inherent property underlying its danger). But it can also not be argued that a very small increase in methionine causes phenyotypical changes of greater magnitude than the like supplementation of any other amino acid. The feeding of a slight excess of tryptophan only caused a reduction in lifespan of 13%, most likely the result of brain serotonin increasing growth hormone. But as brain serotonin is dependent on Fernstromian pharmacokinetics, the ratio likely means more than the absolute amount—and something not liable to get too unbalanced lest one live primarily on lean meat (or is crazy enough to take L-tryptophan supplements). But even then, most anyone with slight immune activation having circulating interferon-γ would be expected to degrade a good amount of any excess tryptophan through the kynurenine pathway, this always induced by the foregoing cytokine through indolamine and tryptophan diooxygenases. I really think methionine can rightly be considered a growth factor: Methionine had caused the rats to balloon and had reduced their lifespans by over a third—and two separate studies by separate and unrelated researchers. I don't think anyone in America has to worry about having 'too little polyamines,' but I still do maintain that many should be concerned about eating too much methionine.

Thank you for this and the two other replies in your thread.
Speaking of threads, I think it's time for one:
Methionine: how low you can go?

 

[Amazoniac]

I've mentioned here that his first book, "Cancer and its allied diseases; their common toxic cause, their cure by immunization" is only available in natioanal libraries, mostly from USA, and i don't have it.

I believe that's the only work his family website doesn't have available for download.

There's 'The chemistry of natural immunity' and there might be others that I'm not aware of.