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1996 Jun;74(6):475-8

The complete absence of dimerization in C396S suggests that Cys396 may be involved in an inter-molecular disulfide bond that results in the formation of an oligomeric structure that combines GSAAT with other enzymes, factors or molecular chaperones involved in ALA formation, such as GluTR, GBP ( The purified UT recombinant GSAAT variants were not entirely reduced, and additional reducing power enhanced their enzyme activities

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Interactions between biosynthesis, compartmentation and transport in the control of glutathione homeostasis and signaling

Glutathione is formed like any other cosmetic or vitamin product in an extremely safe, sterile laboratory setting its manufactured from all-natural amino acids that occur in nature and are useful to our bodies