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I'm not sure, not even one decent Google Scholar result for arugula and nobelium. Also its half-life is at most 1 hour (nobelium, not arugula).Eating arugula is the worst thing you can do for No, add huge amounts of beets and you have quite the cocktail.
AirAmazoniac, what's your diet like?
Thanks for the details. But another important question would be - what is the nutritional value of kale compared to an egg? Can one live off just cooked kale and say coconut oil (or butter)? There was a famous news article making the rounds last year proclaiming a person can thrive on a diet of just potatoes and butter, if they also take a multivitamin to compensate for deficiencies this diet would induce. Btw, I wonder why nobody raised the issue of EFA deficiencies those people on the potato/butter diet undoubtedly experienced...Probably because it was not an issue at all and those people thrived, which would have exposed the EFA scam if the issue was discussed publicly.
So, mashed potatoes with MCT sounds like a good way to avoid most of the toxicities of other food while providing close to 100% SFA.
My only concern with potato juice and large amounts of potatoes in general is the solanine. I dont know if there has been any studies done on the solanine content of potato juice as opposed to mashed etc. It seems to me that the sheer amount of potatoes needed to make any considerable amount of juice would increase the potential solanine burden. Maybe it precipitates along with the starch when left in the fridge overnight? Drinking the pure potato juice without letting it settle sure is revolting after the first gulp or two.. palatability seems way low to me.
I think cooking destroys most of the solanine. To my knowledge Peat never recommended drinking raw potato juice. The cooked mashed potatoes (if peeled) probably do not have much solanine either. Otherwise we would have seen food poisoning cases from eating potatoes, given how toxic solanine is, especially in children.
Yeah he's a "breatharian"Air
And Choline
Tested and approved (awful allergies and asthma, bigger erections). Aragula fresh from mountains located in the South of Italia tastes extremly good though, like sauceless salad with a great sauce. Sometimes the body and the brain want to follow the recommendations of the taste buddies.I'm not sure, not even one decent Google Scholar result for arugula and nobelium. Also its half-life is at most 1 hour (nobelium, not arugula).
But for real, the nitrate content would be brutal indeed.
Not accounted for in cronometer, I think eggs have significantly more biotin, choline and betaine if you consider them important.As far as lipids go: dairy, coconut, beef, chocolate, and fruit all seem good. But for some reason, this forum seems to ignore the substantial linoleic acid content of eggs.
If it is expressed per gram linoleic acid, I would think it would be quite embarrassing to the egg; but I think expressing vitamins and minerals per calorie is the most fair approach. We all eat different volumes and masses of foods, yet everyone eats a very similar amount of calories per body weight.
The cronometer can answer this question with the least amount of work (normalized to 1000‧Cal apiece):
View attachment 8065 View attachment 8066 click to embiggen: Vitamins: Kale on left and egg on right (1000‧Cal).
View attachment 8067 View attachment 8068 click to embiggen: Minerals: Kale on left and egg on right (1000‧Cal).
View attachment 8069 View attachment 8070 click to embiggen: Amino Acids: Kale on left and egg on right (1000‧Cal).
View attachment 8071 View attachment 8072 click to embiggen: Fatty Acids: Kale on left and egg on right (1000‧Cal).
Other than ☀, you're the only other member that has special character, however the artist in question captured the moment while you were sleeping: ☯Yeah he's a "breatharian"
This is a fascinating and bold statement. If this were true, that would make redox balance a very important control mechanism in the cell. To test this claim, I decided to read a short article on aromatase structure:Raypond Meat in his '100 years of cancer metabolism' lensternewt:
"In the first reactions to injury, the inflammatory changes activate enzymes that support undifferentiated growth. The active thyroid hormone, T3, is destroyed locally by a specific deiodinase, prostaglandins are produced by cyclooxygenase, estrogen by aromatase, and nitric oxide by its synthase. These enzymes are activated by chemical reduction of their disulfide groups, converting them to thiols, and can be inhibited by appropriate oxidants. In a healthy organism, those oxidants are available."
There is a russian (translated) book that might interest you a lot, entitled: Sulfhydryl and disulfide groups of proteins - Yu. Torchinskii (ESPN 978-1-4757-0129-6)This is a fascinating and bold statement. If this were true, that would make redox balance a very important control mechanism in the cell. To test this claim, I decided to read a short article on aromatase structure:
Ghosh, Debashis. "Structural basis for androgen specificity and œstrogen synthesis in human aromatase." Nature (2009)
'Unlike the active sites of many microsomal P450s that metabolize drugs and xenobiotics, aromatase has an androgen-specific cleft that binds the androstenedione molecule snugly. Hydrophobic and polar residues exquisitely complement the steroid backbone. The locations of catalytically important residues shed light on the reaction mechanism. The relative juxtaposition of the hydrophobic amino-terminal region and the opening to the catalytic cleft shows why membrane anchoring is necessary for the lipophilic substrates to gain access to the active site.'These quotes are suggestive, and dripping with innuendo. Listen to how he explains how steroids are given wine, and then delicately caressed by aromatose within it's binding pocket—with James Brown music on the turntable!
Four hundred cubic angstroms; any larger a binding pocket they'd have to call it marsupialase!
'The hydrophobic residues and porphyrin rings of hæm pack tightly against the steroid backbone, forming a cavity complementary in shape to the bound steroid (Fig. 2a).'
' The side chains of residues Arg 115, Ile 133, Phe 134, Phe 221, Trp 224, Ala 306, Thr 310, Val 370, Val 373, Met 374 and Leu 477 make direct van der Waals contacts with the bound androstenedione.'
'Androstenedione binds with its β-face oriented towards the haem group and C19 4.0 Å from the Fe atom.'
'The combined surface creates a pocket that encloses the bound androstenedione snugly. The volume of the binding pocket is no more than 400 ų, considerably smaller than the volume of about 530 ų of the active sites in 3A4 (ref. 22) and 2D6 (ref. 23), the two drug/xenobiotic-metabolizing human P450s with highest sequence identities (14–18%) to human aromatase.'
Now: about those thiol groups Ray speaks of:
No talk of a disulfide bridge inactivating this enzyme, and no talk of these thiols being spatially located in a way that would allow disulfide bridge formation upon oxidation. I can find no indication of this enzyme's activity being controlled through the making or breaking of disulfide bridges, but I can picture it as being redox active on account of its porphyrin ring. Imaging perhaps this giant porphyrin ring collecting electrons which eventually shifts to Fe³⁺ forming Fe²⁺, which is the iron species required to bind O₂.
'Having seven cysteines in the reduced form, the bulk of aromatase probably resides in the reducing environment of the cytoplasm.'
The molecular oxygen is though necessary to turn the androgen's methyl group into formic acid (see above). Although depicted as Fe³⁺ in the above graphic, this may not be entirely accurate. The only way to determine the reduction state in the center of heme is through electron spin resonance (ESR); and in the case of phenylalanine hydroxylase, the iron needs to be in the Fe²⁺ state to adsorb O₂. This experiment also shows how an enzyme can be redox active solely through its heme group:
Wallick, D. E. "Reductive activation of phenylalanine hydroxylase and its effect on the redox state of the non-heme iron." Biochemistry (1984)
This enzyme uses the pterin ring as a cofactor, either tetrahydrobiopterin or 6-methyl-tetrahydropterin (used below).
'As with pterin-reduced phenylalanine hydroxylase, the protein locus of the added electron is the iron center. This was shown by titrating Phe-hydroxylase with dithionite [a sulfur molecule] in a system containing the ferrous iron chelator, O‐phenanthroline.' ―Wallick
'In order to determine whether dithionite-reduced phenylalanine hydroxylase is sufficiently activated for catalysis, the cofactor-product coupling experiment was repeated with both phenylalanine hydroxylase, and dithionite-reduced enzyme. The results are depicted in Figure 7, with dithionite-reduced Phe-hydroxylase giving an averaged straight line at 0.93 Tyr/pterin, while Phe-hydroxylase, gave a curved plot of decreasing slope very similar to that expected from Figure 2.' ―Wallick
'Therefore, Phe-hydroxylase [PAH] pre-reduced with one electron/PAH subunit can function catalytically without need to undergo any further reduction by pterin,' ―Wallick
'Since the two-electron oxidation product of dithionite is sulfite, and sulfite is known to act as a two-electron-reducing agent itself (Dixon, 1971a), it was necessary to determine whether product sulfite was serving to further reduce PAH following dithionite reduction of the enzyme.' ―Wallick
'This work shows that a prereduction of Phe-hydroxylase is effected immediately prior to the normal catalytic event. When purified Phe-hydroxylase is added to a reaction system containing phenylalanine, molecular oxygen, and reduced pterin cofactor, stopped-flow spectrophotometry indicates the presence of a pre-steady reduction of Phe-hydroxylase by a stoichiometric amount of pterin, followed by a steady-state catalytic production of tyrosine. It is particularly noteworthy that dithionite can replace pterin in the reduction step as evidenced by observation of the anticipated tight ESR coupling between pterin oxidation and tyrosine formation exhibited by dithionite-reduced Phe-hydroxylase. Thus, addition of only a single electron is necessary for this measure of Phe-hydroxylase activation;' ―Wallick
'The activation of Phe-hydroxylase by prereduction leads to the immediate question as to the locus for the electron furnished by the reducing agent. Since the enzyme contains 1 Fe/subunit, it was essential to characterize the redox state of the iron by examining its spectral properties. The native enzyme displays a composite EPR spectrum, a portion of which has features at effective g values of 6.7 and 5.4 that are similar to, although broader than, features commonly observed in ferric, heme proteins. This spectrum appears to arise from catalytically active ferric iron in a high-spin, S = ⁵⁄₂, tetragonally distorted state whose integrated intensity closely corresponds to the relative specific activity of the Phe-hydroxylase sample. The other portion of the EPR spectrum, with features near g of 9 and 4.3, correlates in intensity with the fraction of catalytically inactive iron. The integrated intensity of the signals in both regions indicates that the iron in Phe-hydroxylase is EPR visible. The EPR signals at g values from 5 to 7 disappear when phenylalanine or pterin are added to the anaerobic enzyme. Since anaerobic incubation of the tetrahydropterin cofactor or phenylalanine with PAH does not result in redox chemistry (Lazarus et al., 1981; Kaufman & Fisher, 1974), the loss of EPR signals cannot furnish information on the prereduction activation (step 1).' ―WallickHe could be talking about singlet oxygen. Oxygen is unique in that it exists in a triplet and a singlet form, and is hence ESR active. Singlet oxygen is blue and is formed in during lipid peroxidation (Kasha, 1970).
'The mechanism requires that the reduction of the Phe-hydroxylase occurs only once at the beginning of the reaction. During the tyrosine-producing event (step 2), the enzyme functions catalytically and requires no further steps to maintain its activity. The view that the Phe-hydroxylase reduction step is a side reaction not related to its catalytic function but serving simply to oxidize cofactor nonproductively may be rebutted by noting that (1) these data mandate the cessation of flux through step 1 after the enzyme is activated since a coupling ratio (tyrosine/pterin) of unity is observed at pterin levels > Phe-hydroxylase (Lazarus et al., 1981; Kaufman, 1971) and (2) our results plus those from pulse-chase experiments demand that unreduced Phe-hydroxylase is largely inactive [Table I1 (Marota & Shiman, 1984)].' ―Wallick
'Several other non-heme, non-iron-sulfur enzymes possess similar types of EPR signals. Protocatechuate 3,4-dioxygenase exhibits EPR signals with prominent g = 4.3 features in the resting enzyme and ones in the region g = 7-5 after addition of substrate (Que, 1980). Soybean lipoxygenase also exhibits multiple signals in the g = 8–5 region after it is treated with 1 mol of its peroxy product, but the resting enzyme is EPR silent (Slappendel et al., 1982).' ―Wallick
'This fact suggests that a reduced iron state, Fe(II)-PAH, trapped by oxygen with formation of an iron–oxygen intermediate, may precede the formation of the actual hydroxylating species. Enzyme-bound iron–oxygen complexes have been well documented, with cytochrome P-450 (Ullrich & Duppel, 1975; Orrenius & Ernster, 1974; White & Coon, 1980) serving as an especially pertinent example of an enzyme that catalyzes hydroxylation reactions via iron–oxygen chemistry. The fact that the prereduction step may be accomplished anaerobically with dithionite provides an approach to investigate oxygen binding to Fe(II)-PAH and subsequent intermediates for the hydroxylation reaction.' ―Wallick
I think this article makes clear that any heme enzyme (i.e. P450s) can potentially be catalyzed by electrons, and thus are very likely redox active. I think this can occur based on the large area or the porphyrin ring, able to spread a delocalized electron across it's entire conjugated superstructure—an electron eventually collected by Fe³⁺, forming Fe²⁺, with subsequent O₂ adsorption and further catalytic activity.
Michael Kasha. "Chemiluminescence arising from simultaneous transitions in pairs of singlet oxygen molecules." Journal of the American Chemical Society (1970)
If this were true, that would make redox balance a very important control mechanism in the cell
Well there's enzymes which use NAD(P)(H) as cofactor, enzymes which glutathione as cofactor, and redox sensitive transcription factors in the nucleus (p53) with disulfide bridges, but I didn't think that cyclooxygenase was redox‐active in the way a person could gather from that Ray Peat quote above—a passage which might seem to imply that aromatase and cyclooxygenase cycled between thiol and disulfide form. I think it's easy to imagine an enzyme in which a disulfide bridge could be created from two thiols in close proximity, blocking the catalytic site and preventing activity.So far I have seen nothing to refute the VERY strong evidence that ANY cancer cells are rather easy to get rid of by simply lowering the GSH/GSSG ratio inside them (and systemically) beyond a certain critical point. GSH is their main protection mechanism against both apoptosis and T-cells. The GSH/GSSG ratio depends on a number of factors but can be lowered by raising the NAD/NADH ratio, eating more sucrose, taking aspirin, quinones, etc.
Do you know of any enzyme/reaction in the organism that is not dependent on NAD (NADH) and/or ATP as cofactors?
Ahh! So the right intestinal bacteria could form polyamines and then donate them to the human intestine in a relay fashion!A question for those that have a cotton factory in your belly buttons:
@TravisAdvances in Microbial Ecology (vol. 6) - K. C. Marshall
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