In vitro study of gamma-glutamyl transpeptidase in rat lens.
gamma-Glutamyl transpeptidase catalyzes the initial step in the utilization of glutathione. In the lens, this enzyme is accessible to externally supplied substrates. An efflux of glutathione from the lens occurs when it was incubated in saline. Inhibition of gamma-glutamyl-transpeptidase by L-serine-borate decreases the rate of glutathione breakdown in the external medium and the rate of its decline in the lens.
D000818:Animals; D005721:Glutamate-Cysteine Ligase / Q000037:antagonists & inhibitors; D005971:Glutamates / Q000494:pharmacology; D005973:Glutamine / Q000031:analogs & derivatives; D005978:Glutathione / Q000378:metabolism / Q000494:pharmacology; D007908:Lens, Crystalline / Q000201:enzymology*; D008717:Methionine Sulfoximine / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D012694:Serine / Q000494:pharmacology; D005723:gamma-Glutamyltransferase / Q000037:antagonists & inhibitors / Q000378:metabolism*
D005971:Glutamates; D005973:Glutamine; D008717:Methionine Sulfoximine; D012694:Serine; C001300:gamma-glutamine-4-nitroanilide; D005723:gamma-Glutamyltransferase; D005721:Glutamate-Cysteine Ligase; D005978:Glutathione