| GSH | <biochemistry> The tripeptide _ glutamylcysteinylglycine. It contains an unusual peptide linkage between the _ carboxyl group of the glutamate side chain and the amine group of cysteine. The concentration of glutathione in animal cells is _5mM and its sulphydryl group is kept largely in the reduced state. This allows it to act as a sulphydryl buffer, reducing any disulphide bonds formed within cytoplasmic proteins to cysteines. Hence, few, if any, cytoplasmic proteins contain disulphide bonds. Glutathione is also important as a cofactor for the enzyme glutathione peroxidase, in the uptake of amino acids and participates in leucotriene synthesis. (18 Nov 1997) |
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| GSR | A change in electrical resistance of the skin, occurring in emotion and in certain other conditions. (12 Dec 1998) |
| GSSG | <chemical> A glutathione derivative that forms when the sulfhydryl side chains of the cysteine residues of two glutathione molecules form a disulfide bond during the course of being oxidised with various oxides and peroxides in cells. Glutathione reductase, with the coupled oxidation of NADPH, reduces gssg to two moles of glutathione. Chemical name: Bis(gamma-Glutamyl-L-cysteinylglycine) Disulfide (12 Dec 1998) |