• N&PD Moderators: Skorpio | thegreenhand

L-glutitione not regarding apap

Grand Touring

Bluelighter
Joined
Apr 5, 2011
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does anyone have any experience with this drug outside the context of eliminating the napqi from the liver after using APAP? The thing that struck me bout it's pharmacology, is that isn't mechanism of action converts the unwanted napqi--lipid soluble byproduct--to a water soluble substance, more easily passed through the liver, and therefore less dangerous.

what peaked my interest is cancelling the lipophilicity of a toxin and allowing it to pass renally. would I be able to use glutitione to convert lipid soluble drugs to water soluble before ingestion. if so, what kind of procedure would have to take place? any cooking? ratios?

thanks for your help, i'll be here all night.

http://www.pointofreturn.com/painkillers.html
 
what peaked my interest is cancelling the lipophilicity of a toxin and allowing it to pass renally

like e.g. HPBCD and the NBOMes?
no, you couldn't. this is because the glutathione molecule is actually reacted with the cmpds being detoxified (enzymes in the liver do this), deactivating them in the process. otherwise glutathione is just like, say, acetylcysetine or something - just a good antioxidant and a polar amino acid.
 
Glutathione gets converted to it's oxidized form GSSG (glutithione disulfide) but yet has the ability to convert back into glutathione because of protein. And the polar amino acid occurs on the surface of proteins which prefer aqueous environments. In layman's terms it takes much more h20 to digest protein, AND L-glutathione DOES NOT convert to norGlutithione. Which still begs the question.
 
Glutathione gets converted to it's oxidized form GSSG (glutithione disulfide) but yet has the ability to convert back into glutathione

Sure. Other sulfur containing amino acids like cysetine will do this too.

because of protein.

Not neccesarily. All that is happening is the glutathione is acting as a redox cycler, like CoQ10 or something. It's oxidised to the disulfide, and the disulfide can be reduced back to plain glutathione by a variety of conditions. This allows Glu to shuttle electrons around.

And the polar amino acid occurs on the surface of proteins which prefer aqueous environments.

It actually occurs in all protiens, polar or not.

In layman's terms it takes much more h20 to digest protein, AND L-glutathione DOES NOT convert to norGlutithione. Which still begs the question.

What are you trying to say here? I don't understand.

Gltuathione doesn't generally react with drugs outside the human body, either - it needs enzymes that are capable of pasting the gltuathione group onto molecules.
 
Okay, so in short Glutathione cannot be used to convert lipid soluble drugs to be used as water soluble, especially not outside the body, correct?
 
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