Methylene Blue Raises Glutathione

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ddjd

ddjd

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wow, thank you so much @Travis you really seem to understand methylation. i just discover that i had sky high serum b12 & folate so i suspect that i under methylate. do you have any advise on what i should do? at the time of the blood work i was taking high doses of iodine(not sure if that means anything) btw, selenomethionine makes me exhausted, does that have something to do with methionine?
Selenomethionine increases my energy. What does this mean?
 

Travis

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Selenomethionine increases my energy. What does this mean?
I think perhaps the most direct, straightforward, and popular explanation would be that it increases the enzyme levels which make thyroxine:

'The discovery in 1991 that Type I iodothyronine 5′‐deiodinase is a selenocysteine‐containing enzyme was of especial interest at the time because this pointed to a biological role of selenium in developmental processes.' ―Stadtman

I think the classic role of triiodothyronine is its ability to increase oxidative metabolism. Finding out if this is indeed true would be easy, as one would only have to ingest thyroid hormone and be on the lookout for similar effects.

But it also creates selenoglutathione. This has a lower—more negative—reduction potential than glutathione, but greater in absolute value since both values are negative (negative since they are accepting electrons).

'Here, we show that GSeSeG and GSSG exhibit a similar difference in bond stability, as the E°′ value of GSeSeG (−407 mV) is 151 mV lower than that of GSSG (−256 mV).' ―Beld

So selenoglutathione has different properties, and would be expected to spend more time in the oxidized dimer form (intermolecular disulfide diselenide bridge). I'm not sure of this would translate to more energy, but it's interesting nonetheless.

Also, the enzyme glutathionine peroxidase is a selenoenzyme.

But selenomethionine can affect enzymes which aren't even official selenoenzymes (which are considered such because they have selenomethionine in the catalytic site). Many transcription factors, like p53, have intramolecular disulfide bonds and are actually redox‐sensitive. During reducing conditions (high e⁻ potential), these disulfide bonds are reduced; this leads to separation of the disulfide bridge (bond):

~C–Se–Se–C~ + 2e⁻ = ~C–Se: :Se–C~ [colon represents two electrons; tilda represents indefinite bond continuation]

Seleonoglutathione affects enzymes differently, as shown below with RNAase:

seleno.png click to embiggen: Graph showing disparate enzyme activities upon addition of either thio‐ or selenomethionine.

And this can effect transcription in other ways as well. The transcription factor p53 is redox sensitive, and will 'activate' (release itself from inactive binding location) itself upon oxidative conditions. So whether or not it incorporates selenomethionine matters, as this will effect the releasing point.

But of course it depends on whether or not the disulfide‐containing enzyme is active in it's oxidized or reduced form. There are many such enzymes which could effect energy, but since you are still eating methionine you wouldn't expect the entire molecule to be 100% selenomethionine; you would have to analyze your methionine intake and compare this to your selenomethionine intake to give an estimation of total bodily selenomethionine:methionine ratio in proteins.

'Although selenium is essential to life, the roles played by this trace element in biological processes are not well understood (33). The majority of characterized selenoproteins are enzymes, which generally show enhanced catalytic efficiency compared to sulfur-containing analogues (7, 8, 34). In selenoenzymes, an active-site selenium often either acts as a nucleophile or performs redox chemistry. For example, it has been proposed that deiodinases utilize a nucleophilic selenolate to convert thyroxine (T₄) to triiodothyronine (T₃) (35), and in the well-studied oxidoreductase glutathione peroxidase, the redox properties of selenocysteine are harnessed in a mechanism that involves conversion of the selenolate to both selenenic acid and selenosulfide-bonded intermediates.' ―Beld

Reading about every selenoenzyme (with catalytic Se‐domain) wouldn't take a particularly long time, but reading about every single enzyme containing a redox‐sensitive diselenide/disulfide bridge would certainly take longer; there are many such enzymes. But trying to explain energy in this manner could represent a lost cause (but interesting nonetheless) considering the fact that selenomethionine would be expected to increase thyroxine synthesis—a much more direct and straightforward explanation.

But it might be helpful to keep the different oxidation–reduction properties of diselenide in mind in case it becomes difficult to explain the additional energy by thyroxine synthesis alone (that is, if observation—either personal or experimental—suggests otherwise).

Beld, Joris. "Selenoglutathione: Efficient Oxidative Protein Folding by a Diselenide." Biochemistry (2009)
Stadtman, Thressa C. "Selenium biochemistry: Mammalian selenoenzymes." Annals of the New York Academy of Sciences (2000)
 
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encerent

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Ray recommends a really tiny does of MB. <1mg. at that does I don't think we'll see any harmful effects.
 
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ddjd

ddjd

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To raise total glutathione levels, supplementing with about 10g glycine for 2 weeks has been shown to work

haidut would love to hear your opinion on this substance "sulforaphane" found in Brassica plants

"Sulforaphane a powerful phytochemical which increases Glutathione Cruciferous vegetables such as cabbage, cauliflower,broccoli, brussels sprouts and turnips are rich in sulforaphane."

i know youre not keen on vegetables per say but supposedly has anti cancer, anti tumor, anti diabetes properties etc.

 
EMF Mitigation - Flush Niacin - Big 5 Minerals

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