Kykeon
Member
- Joined
- Mar 22, 2019
- Messages
- 173
Has someone done the work of archiving travis posts into a readable format or pdf?
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Would anyone be knowledgeable enough to rank grains by the immunogenicity of their proteins? I'm trying a diet where I restrict wheat/dairy proteins, I still consume cream/butter even if they may have trace amounts of them. I'm including oats and white rice and feel good on these sources of carbs.I still think there could be some relationship, as nicotine certainly shares more molecular similarity towards histamine than it does towards acetylcholine. Also, schizophrenics do often smoke. I think nicotine is being used by them as an antidote, and niacin—also found remedial (see Hoffer)—shares molecular similarity with these both. When I had looked at the evidence a few months ago I had become convinced that schizophrenia is best explained by high brain histamine levels. This could very well be due to mast cells which can migrate to the brain; these brain mast cells in turn perhaps consequent of persorbed starch particles in the brain (see Lafora's), brain aluminum (see Alzhemimer's), or the proline-rich and thus enzyme-resistant immunogenic wheat peptides migrating to same location. Brain mast cells have considerable interpersonal variability, ranging from thousands in some to being entirely absent in others. Perhaps people with a TH1-dominated immune system crave cigarettes if they've had them in the past? while those under a TH2-dominated immune state perhaps wouldn't on account of less histamine to antagonize. If a person avoids grains, aluminum, immunogenic proteins, and cortisol, they will very likely have far less histamine to counter—certainly less brain mast cell-derived histamine. The correlation of schizophrenia to wheat consumption–sensitization is also very good, and I think schizophrenia has much more to do with histamine than with the δ-exorphins (the most drug-like molecule characteristic of wheat). There are dozens of 'theories on schizophrenia,' ranging from 'methylation hypothesis' to 'glutamate overload,' and nearly every neurotransmitter has been implicated in this condition (and even some sociological factors). But I am absolutely convinced that not one theory can approach the sum total of evidence directly implicating histamine.
➝ Prell, G. "Histamine metabolites in cerebrospinal fluid of patients with chronic schizophrenia: their relationships to levels of other aminergic transmitters and ratings of symptoms." Schizophrenia research (1995)
Wtf did I just read? Was fun.
too bad ORAC is pro-vaxx where travis was utterly anti-vaxxI found this thread interesting. Doing my own looking around I am find a connection between Travis and Orac, as if they are one in the same Here is a piece Orac wrote.....
Death by intravenous "turmeric": Why licensed naturopaths are no safer than any other naturopath
Naturopaths claim that licensure will guarantee that only naturopaths practicing based on scientific evidence are allowed to see patients. The real situation is that licensed naturopaths are just as quacky (and dangerous) as any other naturopath. This is demonstrated by a recent case in which a...respectfulinsolence.com
Hi,Let me see what the difference is. Luckily, all the dairy exorphins are found in only one location in casein exclusively, not like wheat where there are literally dozens of sequences—the gliadins are highly-repetitive protein—which could be cleaved a certain way yielding one of three known gluten exorphins: gluten exorphin A, gluten exorphin B, and gluten exorphin C. They are often further subclassified by length (i.e. gluten exorphin B5, having five amino acids), but the 'working end'—which always contains an N-terminal tyrosine with ~4 amino acids attached—is always identical among classes and never between them; the only difference then being the elongation of the 'nonworking end' of the peptide, but something which can also affect its activity by either increasing or decreasing the binding affinity and also affecting diffusability, solubility, and partitioning. I think the most active casomorphin is bovine β-casomorphin-5, on account of being the smallest. The longer ones, such as β-casomorphin-11, have also been detected in the cerebospinal fluid and can form all the shorter ones upon enzymatic hydrolysis.
➞ El-Salam, M. "Bioactive peptides of buffalo, camel, goat, sheep, mare, and yak milks and milk products." Food reviews international (2013)
'Peptides of mineral-binding, opioid, angiotensin I-converting enzyme (ACE)-inhibitory, immunomodulatory, cytotoxicity, anticarcinogenic, antibacterial, and antithrombotic activities have been isolated and characterized mainly from cow milk proteins. Variations in the bioactive peptides derived from milk proteins of different mammals can be expected depending on the degree of homology between these proteins. This review focuses on the isolation and characterization of peptides of different bioactivities from milk protein hydolyzates and products of buffalo, camel, goat, mare, sheep, and yak milks.' —El-Salam'Many dietary proteins contain physiologically active peptides encrypted in their amino acid sequences. These peptides are termed bioactive peptides, which remain latent until released and activated by enzymatic hydrolysis.' —El-Salam'Limited studies have been done on the bioactive peptides from milk of nonbovine lactating animals. To our knowledge, information on their bioactive peptides has not been covered in depth in a separate and comprehensive review. Therefore, the present review gives an overview on the bioactive peptides derived from buffalo, goat, sheep, camel, mare, and yak milks.' —El-Salam'Based on the complex nature of goat casein described above, different breeds and even individual animals will produce casein-derived bioactive peptides with different functionalities.' —El-Salam
I like this guys writing, but unfortunately he devotes no attention to the casopmorphins besides a few minor things pertaining to buffalo milk. He instead deals primarily with the angtiotensin converting enzyme (ACE)-inhibiting peptides found. But luckily, there's been one published just this year on sheep casomorphin:
➞ Darwish, A. "Evaluation of β-casein variants in Egyptian goat, sheep and cattle by allele specific PCR and relevance to β-casomorphin." Indian Journal of Animal Research (2018)
'The beta casein gene has 12 genetic variants divided into two groups: the first group (A1, B, and G) which differ from the second group (A2, A3 C, D, E, F, H, H2 and I) where A base replaces C base, this leads to potential liberation of a bioactive peptide, β-casomorphin, upon digestion where a histidine replaces a proline at position 67. The allele specific polymerase chain reaction was evaluated to distinguish between the beta casomorphin releasing variants (A1 and B) and the non-releasing variants. [...] The sequence results reported changing of C base to A base in goat, sheep and cattle. Therefore, this study reported that goat and sheep milk was more safe than cattle milk.' —Darwish'It has been observed in the present study that the highest incidence of the β-casein A1A1 occurred in cattle (22%) compared with goat and sheep (4%).' —Darwish'Consumption of milk having β-casein protein containing A1 and B variants has been implicated in the increasing of diabetes and coronary heart diseases [This here is probably just 'woo,' or a hypothesis gone astray like a balloon in a windstorm. Pauling provides convincing evidence that cardiovascular disease is essentially subclinical scurvy, the arterial collagen not being replaced and remodeled at a sufficient rate. A vitamin C deficiency upregualtes Lp(a) in the liver, which is the lipoprotein most associated with arterial plaques. The body ostensibly does this with the aim of patching and strengthening weak areas of blood vessel wall consequent of low ascorbate, which is senses. Diabetes could have something to do with leucine through the mTOR pathway, something that doesn't change much—if at all—between A1 and A2 varieties. Also not varying greatly is the lipid composition, also related to diabetes. Also: I see no reason to suspect that milk IGF-1 levels would vary between casein variants, even if IGF-1 is actually absorbed whole.]' —Darwish'Sequence analysis: The sequence results showed that C base mutate to A base (C 205 A) in allele A1. Also, goat and sheep beta casein differ from cattle beta casein in SNPs (C4T, G115T, A168G, C192A, C229T, T230G, G279A, T291C, G306A and C313T) and sheep beta casein differ from goat and cattle beta casein in SNPs (G77A, A111T AND A326G) as shown in Figure (3) and summarized in Table 3.' —Darwish'Due to the existence of a histidine in the beta casein protein sequence at position 67 that has the potential to result in cleavage occurring upon digestion and a bioactive peptide, â casomorphin being librated.' —Darwish'The A1 form cleaves at the Ile–His peptide bond during human digestion, to produce the bioactive peptide beta-casomorphin-7. β-casomorphin was detected in all milk samples with the highest amount in A1 milk while there is no BCM7 in A2 milk, which is of potential benefit in human health.' —Darwish'The present study reports that goat and sheep milk is more safe than cattle milk. Therefore, this study recommends the exclusion cattle carrying allele A1 or the dependence on goat and sheep milk. Also, removal of this allele from the national herd by genetic engineering or gene interference may offer benefit for both health and dairy industries; However the consequences of removal of this milk protein variants should first be carefully considered.' —Darwish
The sheep DNA encoding β-casein differed from that of cattle in three places, or two others besides the №67 polymorphism thought responsible for influencing hydrolysis in a way which largely abrogates the opiate potential. However, this study had been done in Egypt; they had used 50 goats, 50 sheep, and 50 cows yet hadn't specified which breeds. The A1∶A2 ratios could very well be higher in the Holstein-dominated United States. Nonetheless: even with his unspecified Egyptian 'cattle,' perhaps being a bit over-representative of Guernsey and Jersey breeds, he'd reported more A1 in the cattle and had even gone as far as recommending its wholesale elimination from the gene pool—or genocide, literally. That's quite the indictment to say the least.
idk if he ever mentioned lean fish, i think he meant raw fish like sushi, but Travis advocated for omega3 intakeWhite rice, potatoes, goat, beef, cheese, spinach, some ocasional lean fish? Ocasional liver, figs, dates, oranges, coconut, dates and ocasional fasting is best, as is intact cholesterol... not too hard to understand?
For calcium? I guess with the amount provided already above, increasing cheese and greens slightly. Coffee is good in moderation
travis's posts on pellagra are very cool. unrelated but ive been wondering why nixtamalization isn't a more common food preparation method, and if it's worthwhile nixtamalizing grains such as buckwheat. i want to try but im hesitant due to the fact that i feel like a lot of nutrients will be lost when washing the buckwheat after soaking. there's probably a reason it's not traditionally done to other grains, the question is if it's due to a lack of necessity, simply due to cirumstances or something else. any thoughts?The process of nixtamalization has actually been shown to partially equalize the amino acid imbalance in corn. Boiling corn in water and calcium hydroxide (or carbonate) makes some proteins less‐soluble, in which they then precipitate to the bottom of the pot. Leucine, considered a factor in pellagra, has shown the greatest reductions relative to other amino acids (~21%). Leucine is also the amino acid found in excess in corn and sorghum—also shown to initiate pellagra. Feeding straight leucine to rats results in an increased excretion of N¹‐methylniacin, perhaps by activating the mTOR pathway, and has also been shown to shift the kyneurine pathways more towards picolinate—at the expense of de novo niacin biosynthesis. The amino acid leucine is unique for being capable of more‐or‐less direct incorporation into the steroid skeleton; if you look at its structure, it's easy to see it nearly as a carboxylated isoprene.
The idea that nixtamalization liberates niacin is a tough sell, since any liberated niacin would of course lost in the water. While true that much niacin is corn is bound to an indigestible polysaccharide (cellulose‐like), this is certainly not unique to corn. All of the rat feeding studies showing increased plasma niacin levels after feeding corn which had been nixtamalized, compared to that which hadn't, could have simply been measuring the effects of ~21% lowered leucine. Thus: the assumed increase in bioavailabilty in such studies could simply be a faiure to understand the mTOR pathway, or actually discovering it without realizing it. The liver has a very specific leucine‐binding protein: a sensor for dietary leucine intake which causes a shift towards cholesterol biosynthesis, ostensibly to make efficient use of excessive dietary leucine by synthesizing cholesterol. I think perhaps the shift in the kyneurenine pathway resulting from excessive leucine could be seen as the body attempting to increase zinc absorption—by synthesizing picolinate—in anticipation of more cholesterol. Either that, or you probably have to assume the body simply malfunctions as a result of excessive leucine—something harder to imagine when realizing that the body has it's own sensor for dealing with this essential amino acid.
I do add calcium hydroxide to pasta. First I boil the pasta in water and salt and once the pasta is soft I add a teaspoon of calcium hydroxide and boil a few minutes more. The pasta turns yellow and has a slightly eggy/sulfuric smell that is reduced after washing the pasta in cold water. The taste is a little bit different, a whiff of eggs which might explain the lack of popularity of nixtamalization of other grains than corn. I find it more digestible though.travis's posts on pellagra are very cool. unrelated but ive been wondering why nixtamalization isn't a more common food preparation method, and if it's worthwhile nixtamalizing grains such as buckwheat. i want to try but im hesitant due to the fact that i feel like a lot of nutrients will be lost when washing the buckwheat after soaking. there's probably a reason it's not traditionally done to other grains, the question is if it's due to a lack of necessity, simply due to cirumstances or something else. any thoughts?