The Travis Corner

[Wagner83]

[...]
Although having superimposable names, the bromelain of the stem is in fact a different protein than the bromelain of the pulp.

'Stem-bromelain (EC. 3.4.22.32) is distinguished from fruit-bromelain (EC. 3.4.22.33), previously called bromelin [2].' ―Maurer

'The substrate spectrum is similarly broad, extending from synthetic low molecular mass amides and dipeptides up to high molecular substrates such as fibrin, albumin, casein, angiotensin II, bradykinin. Bromelain preferentially cleaves glycyl, alanyl and leucyl bonds.' ―Maurer​

So we are not limited to collagen. Bromelain appears capable of cleaving peptide bonds at short‐chain nonpolar amino acids. No mention is made of proline, and due to the unusual nature of the prolyl peptide bond the omission of such could perhaps be taken as synonymous with 'it don't.'

Even better than the opiate effects, they reduce antigenicity. For a peptide to be an antigen, is has to be over about 8–11 amino acids long. The fact that taking such enzymes reduces the interferon-γ spike that can be observed in some people after injesting gluten is another proof that these enzymes hydrolzye peptides into smaller fragments.

Now we do have such enzymes, on the intestinal brush border. However, sometimes—and perhaps from inflammation—the activities of the enzymes are obviously insufficient to hydrolyze all proline‐rich peptides. All of the experimental evidence accrued dealing with prolyl endopeptidase enzymes centered around the slightly larger immunogenic fragments.

But you would expect the opiate effects to be reduced proportionally.

I think they are safe, but the enzyme bromelain has shown to be absorbed as a high‐molecular weight species. But this is not necessarily a bad thing, as circulating prolyl proteases could help cleave circulating opiates. We already have one such circulating enzyme, called dipeptidy peptidase IV, which ostensibly plays a role in all of this. Perhaps low activity alleles are associated with exorphin sensitivity?

According to U.S. Patent № 6,251,391, circulating prolyl peptidases are thought to reduce circulating opiates.

Wilkinson, Randall Eugene. "Compositions containing dipepitidyl peptidase IV and tyrosinase or phenylalaninase for reducing opioid-related symptons." U.S. Patent № 6,251,391 (2001)​

Interesting background on autism:

'Analysis of the urine of autistic children found hyperpeptiduria in the children, which means that the analysis found a significantly increased presence of peptides, in this case the exorphins casomorphin and gluteomorphin, in the urine of children. Reichelt et al. (1990); Reichelt et al., Brain Dysfunct., 4:308-319 (1991); Reichelt et al. (1994). Reichelt et al. (1994) hypothesized that the peptiduria was caused by insufficient breakdown of casein and gluten. Reichelt et al. (1991), at 308, also hypothesized that the release of the opioid-like casomorphin (from casein) and gluteomorphin (from gluten) were caused by a defect of peptidases in the patient. Accordingly, Reichelt et al. proposed a strict gluten-free and casein-free diet (i.e., strictly wheat-free and dairy-free). Reichelt et al. (1990) found that such a diet ultimately resulted in increased social contact, decreased stereotypy, an end to self-mutilation like head banging, and a decrease in dreamy state periods. Also, alimentary problems generally improved. Reichelt et al. (1990) at 5; accord Reichelt et al. (1991); Reichelt et al. (1994).' ―Wilkinson​

'Ackerman (1997) hypothesized that the addition of papain, bromelain, and chymotrypsin to the diet of the patient might be beneficial. However, Ackerman never reported the actual use of any such enzymes, and his proposed combination would not be expected to work because chymotrypsin, according to Reichelt et al. (1994) at 79, is one of the digestive enzymes (as well as trypsin and the hormone secretin) believed to release the detrimental opioid sequences. Papain and bromelain are, likewise, broad-spectrum digestive enzymes that would also have a reasonably high chance of actually increasing the amount of opioids, i.e., casomorphins or gluteomorphins, instead of reducing them (absent the additional use of an agent to specifically inhibit the casomorphin or gluteomorphin, as discussed further herein).' ―Wilkinson​

Interesting stuff:

'Read labels—items like bread and tuna fish often contain milk products. [?]' ―Wilkinson​

While reading food labels is always a good idea, going to grocery stores which put milk in tuna fish is not.

The patent holder shamefully appeals to emotion; judge breaks‐out in tears; this should perhaps be rewritten or his patent revoked:

'When administered to human patients suffering from autism, without restriction on the normal diet of the patients, the compositions and methods reduced one or more symptoms of autism, such as increased eye contact, better enunciation and use of pronouns, less fatigue, singing a song for the first time with the melody and words together and the entire song understandable, playing with age appropriate friends for the first time, fewer tantrums, better sleep patterns, improved politeness and coordination, being more loving, acknowledging another individual's emotion, increased voice and word association and, in one case, noticing that a calendar needed changing. [He forgot to add 'frolicking through a field of daisies in the springtime with bunnies and fawns' and 'dutifully mastering the piano at an early age with one hand while painting van Dyck replicas with his other.'] In addition, the present invention provides compositions and methods that inhibit gluteomorphin and casomorphin, and other exorphins, from sources other than casein and gluten, which assists in the treatment of the exorphin-related diseases for persons that are already wheat-free and dairy-free, yet are still ingesting, or otherwise taking in, exorphins from other sources.' ―Wilkinson​

Now for the important stuff:

'In a preferred embodiment, the casomorphinase is a proline protease, further preferably a protease comprising the dipeptidase activity of dipeptidyl peptidase IV.' ―Wilkinson​

Be he doesn't seem to present any evidence that this will work. But theoretically, you could be almost certain that it would—it really ought to.

And with the supplementation of commercial enzyme capsules around the time of consumption—such as those containing bromelain or prolyl endopeptidase—all dangerous peptides should be deftly broken down into individual amino acids or harmless short di- and tri-peptides. After eating bread in that way, you'd only then have to worry about the reduced iron and aluminum that it might contain (read label).

There's actually been a study on bromelain showing it can hydrolyze gluten to the point of it being completely nonimmunogenic. Papain has actually been more thoroughly studied, as it seemed to have been more of a standard 'research chemical' a few decades ago, but with conflicting results. Initial reports showed that it completely hydrolyzed gluten, but a later investigator had showed that it didn't do anything besides an insignificant deamination of glutamine to glutamate. Later articles had proposed the explanation that only 'crude papain,' as was used initially, was able to do this and purified papain is largely inactive. Crude papain contains many other enzymes than simply papain, yet is still called 'papain,' and is a material which represents the unresolved dried latex exudate from scored green papayas. The papain for sale in grocery store is likely purified and crystallized papain, and I wouldn't expect it to work based on the studies I had read. However, I would expect bromelain to work.

@Travis I recklessly butchered your posts but encourage anyone interested in them to click on the arrow and go read them in their entirety. I'm considering adding bromelain to gelatin (and generally speaking, to meals) before eating and see how I fare with it since I've had issues when it was simply dissolved in hot water. After all the activity of bromelain is measured in GDU, gelatin digestive units, so it should help. If I understand correctly does the first quote means bromelain wouldn't be able to reduce the opiate effects of dairy because it doesn't affect proline bonds? I guess instant decaffeinated coffee (e.g. for those who don't want caffeine at night) would be a good idea.

 

[Travis]

You doubt that pomegranates and dates are high in phytoestrogens or that those phytoestrogens are comparable to regular estrogens or perhaps the estrogens in soy?

Yes. I have seen panels of polyphenol binding data on the estradiol receptor, both using types α and β. Now despite the scientific evidence showing otherwise, why are you insinuating that a plant polyphenol—any plant polyphenol—besides daidzein and genistein can even be considered a 'weak estrogen?' even charitably so?

No hypocrisy, I don’t consume dairy, I have issues with the opiate effect which I have written about on this forum (I think prior to your post on this) as well as read from you in regards to the prolactin stimulating aspect. Also, I mentioned nothing about gyno. I don’t consume eggs or whey either, [...] I dont eat any grains currenlty [sic]

Now what exactly do you eat then?

CLASH's food avoidance list:

☑Dairy

☑Fruit

☑Vegetables

☑Grains

☑Eggs​

As for the more specific points your going to have to give me time to really refute them adequately.

Don't bother. You cannot just 'refute' the truth willy-nilly, simply wave a magic wand, and then proclaim that now myricetin is a potent 'phytoestrogen.' Likewise, conjuring unrealistic serotonin pharmacokinetics will in no way advance anyone's understanding; the more pertinent talk—for those concerned about brain serotonin and not peripheral platelet serotonin—will always be focused on the Fernstrom ratio. It has been proven a long time ago that plasma albumin-bound tryptophan will more readily cross the blood–brain barrier than will platelet-bound serotonin. Peripheral serotonin is not generally thought to significantly contribute to brain serotonin.

Lastly, what about the other points I have presented?

Well, if I had actually seen any.. .

 

[Travis]

@Travis I recklessly butchered your posts but encourage anyone interested in them to click on the arrow and go read them in their entirety. I'm considering adding bromelain to gelatin (and generally speaking, to meals) before eating and see how I fare with it since I've had issues when it was simply dissolved in hot water. After all the activity of bromelain is measured in GDU, gelatin digestive units, so it should help. If I understand correctly does the first quote means bromelain wouldn't be able to reduce the opiate effects of dairy because it doesn't affect proline bonds? I guess instant decaffeinated coffee (e.g. for those who don't want caffeine at night) would be a good idea.

I think it very well could. It might cleave casein in such a way as to prevent β-casomorphin formation. Of course all amino acids would still be present but the order in which they end-up makes all the difference. But since bromelain had been shown to completely abrogate the immunogenicity of wheat flour, before baking, then it might actually be a legitimate prolyl peptidase (gluten being very rich in proline). I don't think this has ever really been tested thoroughly, and I've looked; but I do think there are some detailed articles about what peptide bonds it preferentially cleaves, or between which two amino acids.

Bromelain is great, and has consistently been shown to reduce prostaglandins. The mechanism is never explained entirely but as a protease, I think you'd have to assume that it's breaking down some protein or another (although oddly, there are mechanisms unrelated to its proteolytic function). I think the most popular idea is that it breaks down fibrin, reducing inflammation by facilitating lyphatic flow (by viewing 'swelling' a a localized increase of extracellular fluid). But it could also hydrolyze immunogenenic peptides in the circulation, break-down cytokines, or perhaps even cleave-off the receptors for them (on cell membranes).

Another interesting thing about bromelain is that it proves that proteins large enough to actually be enzymes can and will be absorbed intact, and in a fully-functional form. Of course nature designs bromelain to be acid-stable, but I think this still could have implications for bovine IGF-1 and insulin. I would avoid homogenized milk as this mechanical process has been shown to encapsulate bovine xanthine oxidase into liposomes, thereby allowing for its complete absorption by protecting it:

Zikakis, J. "Persistence of Bovine Milk Xanthine Oxidase Activity after Gastric Digestion In Vivo and In Vitro." Journal of dairy science (1977)​

 

[CLASH]

@Travis
I dont appreciate the twisting of my words into generalized statements to purposely misinterpret what I am saying and discredit me. I am not argueing against your point of view, I am simply trying to converse with a knowledgeable person in a respectful way about some of my experiences that seem counter to their knowledge base.

With all the knowledge you seem to have its a bit unnerving to see your reaction to any points that are somewhat counter to yours even when they are presented in a friendly manner. Atleast for me, the way with which you interact to points counter to your point of view undermines your credibility. Thanks for your time with this conversation, I am not interested in continuing it with you. In the future if I have any questions that fall directly in line with your belief system I’ll reach out.

 

[Wagner83]

I think it very well could. It might cleave casein in such a way as to prevent β-casomorphin formation. Of course all amino acids would still be present but the order in which they end-up makes all the difference. But since bromelain had been shown to completely abrogate the immunogenicity of wheat flour, before baking, then it might actually be a legitimate prolyl peptidase (gluten being very rich in proline). I don't think this has ever really been tested thoroughly, and I've looked; but I do think there are some detailed articles about what peptide bonds it preferentially cleaves, or between which two amino acids.

Bromelain is great, and has consistently been shown to reduce prostaglandins. The mechanism is never explained entirely but as a protease, I think you'd have to assume that it's breaking down some protein or another (although oddly, there are mechanisms unrelated to its proteolytic function). I think the most popular idea is that it breaks down fibrin, reducing inflammation by facilitating lyphatic flow (by viewing 'swelling' a a localized increase of extracellular fluid). But it could also hydrolyze immunogenenic peptides in the circulation, break-down cytokines, or perhaps even cleave-off the receptors for them (on cell membranes).

Another interesting thing about bromelain is that it proves that proteins large enough to actually be enzymes can and will be absorbed intact, and in a fully-functional form. Of course nature designs bromelain to be acid-stable, but I think this still could have implications for bovine IGF-1 and insulin. I would avoid homogenized milk as this mechanical process has been shown to encapsulate bovine xanthine oxidase into liposomes, thereby allowing for its complete absorption by protecting it:

Zikakis, J. "Persistence of Bovine Milk Xanthine Oxidase Activity after Gastric Digestion In Vivo and In Vitro." Journal of dairy science (1977)​

Thanks!

Do you know if adding the bromelain to the cheese a while before eating would be better than simply mixing them in the stomach (where bromelain may not have as much time to work its magic before the opiate effects occur)? Bromelain is used for sinusitis so this an other reason to consume it with dairy since, as you explained and as a few noticed before, it can have mucogenic properties.

 

[Obi-wan]

@Travis said "Bromelain is great, and has consistently been shown to reduce prostaglandins" That's all I needed to hear. I now take Bromelain after every meal

 

[Amazoniac]

You know, same original class joke as always.

Most medical doctors, and even to this day (and the ones who actually read of course), very likely stick to only a few different journals (i.e. BMJ, The Lancet) they have floating around the office. Take just the first thing to come to mind as an example: Docosohexanoic acid. A person can compare clinical MRI scans (showing white matter in the grey matter) from a medical journal with in vitro steroid exclusion studies using artificial liposomal membranes from a physical chemistry journal—from the hard chemists with all their more precise language, instruments, and honesty out of simple respect for their scientific discipline. So you can then infer things about DHA's ability to exclude cholesterol from one study into the myelin ingression seen in Zellweger's disease—via MRI—read in a seemingly-unrelated journal resulting in novel interconceptual linkages; add to that a few biochemical articles from yet other disparate journals rarely found in even the same University library as the others—perhaps on the lipogenic enzymatic pathways—and you can distill them all down into bite-sized heuristic articles having a strong core mechanism fully-supported by published evidence (and all the while using impeccable logic). By being one of the few people who read a good number of trans-disciplinary articles, a person will naturally make novel connections without even having the intent of doing such.

And it looks as if we've gone full-circle; below I am writing about γ-tocopherol again:​

¶ If I were charged with making a television advertisement for γ-tocopherol—which powerfully traps and filters inhaled nitric oxide I should add—it would be a historical facetious one set in 1944 Aushwitz: After the gas had cleared the chamber and the officers had entered—to clear the 'kindling'—the Staffelführer looks amazed to find one inmate still alive, and standing: 'Wha―! What's your secret,' he asks. The lone Jew winks, smiles, and laughs maniacally. [Image pans-out with stern voiceover: 'From Zyklon-B to diesel exhaust, γ-tocopherol from Tropical Holistic™ will radically-protect your lungs from damaging environmental gasses.']
​

Serotonin can make a person tired, but I think the melatonin wave which comes later will increase creativity (but always at the expense of other virtues; a person can have multiple personalities, but of course can only express them one-at-a-time).

Oleamide is the sleep-inducing sensor of plasma ammonia levels: High levels of plasma ammonia are invariably associated with somnolence and stupor, yet the chemical mechanism is never logically explained. It has been shown that brain oleamide synthesis is a linear function of oleic acid and ammonia concentrations, making oleamide a veritable plasma ammonia sensor; this links liver damage and also heavy food intake—along with the Fernstrom Ratio—with drowsiness, and could be the very molecular representation behind the oft-mentioned 'gut–brain axis.'

Carnivores do tend to get tired after they eat, something I've heard explained by 'increased blood flow to the digestive organs.' But does this actually even happen, despite its simplistic and intuitive appeal?

'Malnutrition, and specifically protein deficiency, produces an inflammatory state that involves extreme serotonin dominance. Stress or malnutrition prenatally or in infancy leads to extreme serotonin dominance in adulthood. Other functions of tryptophan are reduced, as more of it is turned into serotonin.' —Ray Peat​

Fernstrom showed that his eponymous ratio is what best predicts brain tryptophan uptake, and hence brain serotonin synthesis, and far better than the either the absolute tryptophan concentration or even the free tryptophan concentration. A lack of protein tends to increase the Fernstrom ratio as tryptophan has an higher affinity for the bloodstream than most others (probably all others) on account of serum albumin having seven high-affinity tryptophan-binding domains—one for each α-helix. The brain has a region of microcirculation where albumin is 'squeezed,' lowering the tryptophan–albumin affinity as measured in vitro. This has been proven by injections or radiolabeled tryptophan quickly followed by decapitation, and first-pass brain uptake of albumin-bound tryptophan is substantial—much greater than predicted from in vitro dissociation constants. Insulin lowers the tryptophan ratio by inducing cells to internalize amino acids, drawing them out of circulation. It is in this way that a protein-free high glycemic acid food (i.e. Red Bull™, candy, Mountain Dew™) will raise brain serotonin, as explained by Fernstrom (the World's leading expert in tryptophan pharmacokinetics, as far as I'm concerned).

'Malnutrition' can be a low protein state when not accompanied by interferon-γ (which induces indolamine diooxygenase, tending to lower serotonin). A person eating a low protein diet while having preparation techniques that attenuate the allergenicity of any ingested grains could be expected to have a high Fernstrom ratio. However, their lack of blood ammonia and oleic acid consequent of malnutrition would tend to counteract this to a degree (see Oleamide: The one-and-only serotoninergic lipid).

As the serotonergic effect of 'malnutrition' can be explained by Fernstrom kinetics, that of 'overnutrition' can be explained by Travis kinetics. Exceedingly high protein consumption can lead to hyperammonemia; and this, working in tandem with oleic acid—usually a nonproteomic indicator of a high protein diet—and an upright posture, can increase brain NH₄⁺ uptake and subsequent oleamide synthesis. This lipid allosterically binds at least three serotonin receptors (5-HT₁, 5-HT₂, 5-HT₇), commonly increasing the measured response fivefold at nanomolar concentrations.

Thus, the best brain state would be neither 'malnutrition' nor 'overnutrition;' this is both true biochemically as it's defined semantically, as such. To keep serotonin in-range, the intake of: tryptophan, oleic acid, competing amino acids, and free carbohydrate need to be considered. High protein diets and liver damage can increase the plasma NH₄⁺ concentration, leading to non-Fernstrom serotonergic effects consequent of oleamide.

[*] I do realize that NH₄⁺ is ammonium, and not 'ammonia,' yet values for serum ammonium concentration are most often incorrectly given as 'plasma ammonia levels.' Ammonia (NH₃) is basic, and when placed in water it takes a proton from solution (H⁺) forming ammonium (NH₄⁺). In a similar manner, carboxylic acids (i.e. citric acid, malic acid) always lose a proton in solution forming the carboxylate anion (i.e. citrate, malate). Nonetheless, many people speak of plasma citrate as if it were literally 'citric acid.' This isn't a very big problem as long as people do not become confused and are aware of the fact that amines and carboxylic acids are nearly always ionized in aqueous solution. ​

 

[Travis]

Thanks!

Do you know if adding the bromelain to the cheese a while before eating would be better than simply mixing them in the stomach (where bromelain may not have as much time to work its magic before the opiate effects occur)? Bromelain is used for sinusitis so this an other reason to consume it with dairy since, as you explained and as a few noticed before, it can have mucogenic properties.

Perhaps could be on account of it's three chitinases? These enzymes are named for degrading chitin, a somewhat unusual polysaccharide synthesized by yeast and crustaceans. In yeast, chitin forms an indispensable structural component of their cell wall. Vertebrates do not synthesize chitin, and nor do plants, so the discovery that humans actually encode for two chitinases may initially be surprising. Like nitric oxide synthase and cyclooxygenase, we do have two chitinase forms: a constitutive one always similarly expressed (AMCase), and another induced by cytokines (chitotriosidase). The constitutive chitinase is primarily found in the stomach and airways ostensibly to protect against spores, while the inducible one in found in the circulation and released by natural killer and T-cells. These enzymes protect people against yeast by hydrolyzing chitin on their cell wall; chitinases represent yet another class of polysaccharide-hydrolyzing enzymes in humans, besides the amylases for starch of course (and the cellulases for cellulose).

Taira, T. "Tissue distribution, synthesis stage, and ethylene induction of pineapple (Ananas comosus) chitinases." Bioscience, biotechnology, and biochemistry (2005)​

Mucus is a polysaccharide gel, so you'd imagine the degree of carbohydrate chain branching and also their length would determine its viscosity. Commercial bromelain tablets include a crude pineapple extract in which a chitinase has also been determined. This finding adds a bit of ambiguity to nearly all clinical bromelain studies, whose authors were apparently unaware of any other enzymes present. Instead: they had invariably assumed 100% of any observed or reported change had derived from stem bromelain, or the main protease. But since you'd also expect a good deal of chitinase in these tablets, simply attributing all inflammatory activity to stem bromelain now appears presumptuous.

Hung, T. "Purification and characterization of hydrolase with chitinase and chitosanase activity from commercial stem bromelain." Journal of agricultural and food chemistry (2002)​

And since pineapples have powerful enzymes for hydrolyzing polysaccharides, it could potentially even be effective against lipotoxin—consisting primarily of lipid and polysaccharide. As a main 'inflammatant,' lipotoxin and pineapple could be something to look into. But just remember: All clinical studies using crude bromelain are confounded by substantial levels of chitinase activity unkowingly given.

 

[Obi-wan]

I have read that Fungi can be found in all cancer cells and the mutated cancer cell incorporates Chitin into its cell wall

 

[Travis]

@Travis said "Bromelain is great, and has consistently been shown to reduce prostaglandins" That's all I needed to hear. I now take Bromelain after every meal

Don't forget about the γ-tocopherol—this is huge. Gamma-tocopherol is ideally-suited to trap both peroxynitrite and nitrogen dioxide from cigarettes, automobile exhaust, and that produced in the body. Besides the more substantial vitamin E activity that α-tocopherol had shown in the fetal (rat) absorption assay, the primacy of the flagship (α) subform had been further supported by the finding that humans have higher plasma α-tocopherol levels despite consuming a similar amount of γ-tocopherol. Seen historically as a more ancillary subform, perhaps 'the escort of the fleet,' the supposed insignificance of γ-tocopherol is immediately shattered by three important observations: Gamma-tocopherol has a much higher turnover rate than α-tocopherol; gamma-tocopherol can bind and deactivate reactive peroxinitrite far more effectively than the other the tocopherols; its de-alkylated metabolite abbreviated γ-CEHC is ubiquitous, functional, and biologically-active. As having the same head group, carboxyethyl-6-hydroxychroman can absorb peroxynitrite just as well as γ-tocopherol; the only important difference between two is disparate solubility and partitioning characteristics, with γ-tocopherol being necessarily membrane-bound and γ-CEHC existing in the water-phase. Since the main function γ-tocopherol and its docked-tail congener can rightly be assumed to be 'for detoxifying nitrogen dioxide and peroxynitrite,' it follows that perhaps smoking would deplete serum levels:

Brown, A. "Acute effects of smoking cessation on antioxidant status." Journal of nutritional biochemistry (1996)​

‘These results point to a special relation between γ-tocopherol and smoking status and indicate that increases in plasma antioxidant vitamins can be detected very soon after the cessation of smoking.‘

‘For plasma lipid-soluble antioxidants of the cessation group there was a significant rise observed for γ-tocopherol when the values were expressed as a percentage difference. ‘

‘Furthermore, the increase in plasma γ-tocopherol was related to the self-reported number of cigarettes smoked per day at entry to the study.'

‘Gamma-tocopherol increased significantly in the LDL fraction after smoking cessation as did α- and β-carotene. On average, LDLγ-tocopherol increased 40% above that seen in the control group.’

‘Previous studies have mostly included γ-tocopherol as part of total vitamin E or only reported on a-tocopherol levels. ‘

‘In the present study, the increase observed in plasma and lipoprotein γ-tocopherol after stopping smoking is a novel finding. That this increase was directly related to smoking status was given further credence by our finding that γ-tocopherol was lower in smokers than nonsmokers. Moreover, the rise in plasma γ-tocopherol was positively related to self-reported cigarette consumption at entry to the study.’

‘it is conceivable that γ-tocopherol might be ideally suited to protect us against smoking-induced damage.’

‘Furthermore, plasma γ-tocopherol was found to be lower in smokers than nonsmokers.‘​

 

[Travis]

I have read that Fungi can be found in all cancer cells and the mutated cancer cell incorporates Chitin into its cell wall

Very interesting. Do you remember where you had read that? This is important, because chitin synthesis (in Candida albicans) requires both glucose and glutamine to produce N-acetylglucosamine (or it could use this molecule directly, as from a supplement). This fact means that grains are especially troublesome in this regard, as these foods have extremely-high glutamine levels. Seeds in general store very high amounts of easily-retrievable nitrogen for germination as either glutamine or asparagine. All grains and many seeds have very high glutamine concentrations, while legumes and tree nuts have similarly-high asparagine concentrations. The exact concentrations can be tracked-down in some cases, but this data is relatively hard to find. For one, standard dietary amino acid composition charts do not include glutamine; when they do include it, it is listed under 'glutamate.' The main reason for this is that acid hydrolysis—the proteolysis done before amino acid sequencing—converts glutamine and asparagine into glutamate or aspartate, respectively. [Free ammonia is released from this, which can be used to estimate the total Gln + Asn concentration.] Another reason is the similarity in the mass spectra between the two, and HPLC-MS is one of the most common ways to determine amino acid composition. Only more elaborate techniques will differentiate between glutamine and glutamate.

 

[Travis]

@Travis
With all the knowledge you seem to have its a bit unnerving to see your reaction to any points that are somewhat counter to yours even when they are presented in a friendly manner. Atleast for me, the way with which you interact to points counter to your point of view undermines your credibility. Thanks for your time with this conversation, I am not interested in continuing it with you. In the future if I have any questions that fall directly in line with your belief system I’ll reach out.

Thanks. But please don't act as if I had been pleading to interact with you . . . or that you'd actually been doing me a favor by parroting those same unrealistic anti-vegan talking points that I've heard dozens of times before—spreading irrational fear, uncertainly, and doubt about the most-natural foods and then dodging my inquiry into what you eat (which cannot be much of anything, really, without contradiction; you have denied eating nearly everything.)

 

[Braveheart]

Cancer/fungus.... This Italian Doctor Simoncini has long talked about this...you have to dig for more info...there's a lot out there...they chased him like Koch etc. I have kept serious keratosis at bay since I took his advice...iodine on my skin/fungus? cancer. Don't know if this applies to the foregoing posts...but should be interesting to research, no? Connect some dots...exciting this!

The Simoncini Treatment of Cancer

Cancer is a fungus, called candida, says Dr Simoncini

 

[Travis]

Cancer/fungus.... This Italian Doctor Simoncini has long talked about this...you have to dig for more info...there's a lot out there...they chased him like Koch etc. I have kept serious keratosis at bay since I took his advice...iodine on my skin/fungus? cancer. Don't know if this applies to the foregoing posts...but should be interesting to research, no?

I've heard about Simoncini, and had just thought of him a few minutes ago (inspired by the chitin–cancer comment). I certainly intend on looking into this because I've already read a bit about chitin synthesis. This polysaccharide is not at all produced by humans, nor plants, so the only way it could get into the body is through yeast or by eating lobsters. Chitin has glycosidic-β-linkages and is tough like cellulose. Adding N-acetylglucosamine, the lone monosaccharide of chitin, powerfully induces the yeast ⟶ hyphal transition of Candida albicans; there have been at least five studies proving this as the central focus, with dozens more using acetylglucosamine in an offhand and now-routine manner for inducing the hyphal form. Mycelial Candida albicans has five times more chitin than has the yeast form; the hyphae, what actually defines the mycelial form, are especially enriched in chitin. Thus: small amounts of chitin are indispensable for C. albicans and hyphal growth is made possible only with access to substantial amounts of chitin precursors: acetylglucosamine, or glucose plus glutamine (through the agency the enzyme glucosamine-6-phosphate synthase).

I've tried adding more whole cinnamon bark to my coffee after having used just a bit previously, which I didn't like. But I had the idea that the coffee + cinnamon combination could be characterized by what I'd call a 'counter-intuitive mixing effect.' This does appear to be true: using a lot of cinnamon tastes good, as does using none at all, despite the fact that coffee is made worse by using just a little. I think you'd get a U-shaped curve if taste were to be plotted against added cinnamon bark.

Materials & Methods: Seven hundred milligrams (dry weight) of outer bark peeled from Cinnamomum verum was added to a French press containing fifty grams of coffee ground coarse; This had been given to group A₁. Groups A₂–A₇ then had been given same dose coffee having progressively graded amounts of cinnamon bark. The other groups had been given 300·mg more cinnamon than the one which had proceeded it, maintaining the ordinal sequence, done to prevent the inter-group taste-habituation effects first observed by Willoughby et. al. [14] consequent of using escalating doses within the same group.

Results: A striking and counter-intuitive mixing effect was observed resulting in a U-shaped cinnamon response curve [Fig 3.], the A₇ group reporting a rather pleasant all-around experience comparable with that reported from group A₁. Groups representing the intermediate doses.. .​

 

[Braveheart]

years ago I was on the chitin bandwagon...but can't remember exactly why?!
Applications of Chitin and Its Derivatives in Biological Medicine
Chitin health benefit and medical uses

 

[Braveheart]

years ago I was on the chitin bandwagon...but can't remember exactly why?!

Applications of Chitin and Its Derivatives in Biological Medicine

Chitin health benefit and medical uses

 

[Obi-wan]

Very interesting. Do you remember where you had read that? This is important, because chitin synthesis (in Candida albicans) requires both glucose and glutamine to produce N-acetylglucosamine (or it could use this molecule directly, as from a supplement). This fact means that grains are especially troublesome in this regard, as these foods have extremely-high glutamine levels. Seeds in general store very high amounts of easily-retrievable nitrogen for germination as either glutamine or asparagine. All grains and many seeds have very high glutamine concentrations, while legumes and tree nuts have similarly-high asparagine concentrations. The exact concentrations can be tracked-down in some cases, but this data is relatively hard to find. For one, standard dietary amino acid composition charts do not include glutamine; when they do include it, it is listed under 'glutamate.' The main reason for this is that acid hydrolysis—the proteolysis done before amino acid sequencing—converts glutamine and asparagine into glutamate or aspartate, respectively. [Free ammonia is released from this, which can be used to estimate the total Gln + Asn concentration.] Another reason is the similarity in the mass spectra between the two, and HPLC-MS is one of the most common ways to determine amino acid composition. Only more elaborate techniques will differentiate between glutamine and glutamate.

Read it in Ron Gdanski's Book: Cancer Cause, Cure, and Cover-up. Page 32 "All human cancers are caused by the incorporation of chitin into the cell-wall membrane of human cells during mitoses"

 

[Obi-wan]

Still not sure of the soybean and sunflower oil content

 

[Nighteyes]

I started using Jarrow's Gamma E after Tocovit ran out :) Great product and nice amber colour - although I am not sure if this is not just due to the "organic caramel"

Jarrow Formulas : Gamma E

 

[Obi-wan]

I started using Jarrow's Gamma E after Tocovit ran out :) Great product and nice amber colour - although I am not sure if this is not just due to the "organic caramel"

Jarrow Formulas : Gamma E

Other Ingredients
Softgel consists of gelatin, glycerin, purified water and organic caramel.

No wheat, no gluten, no dairy, no egg, no fish/shellfish, no peanuts/tree nuts.

This could be the one!