Properties of gamma-glutamyltranspeptidase, and glutathione levels in rat mammary gland.
gamma-Glutamyltranspeptidase activity and glutathione levels were studied in rat mammary gland during the lactogenic cycle; both increased during mid-lactation. The enzyme's specific activity with several amino acids showed that glutamine and methionine were the best substrates. Maleate decreased the transpeptidation reaction and increased the hydrolytic activity. These results suggest that gamma-glutamyltranspeptidase from the mammary gland is similar to the enzyme described in other tissues in relation to these properties and the physiological role proposed in amino acids transport.
D000596:Amino Acids; D000818:Animals; D005260:Female; D005978:Glutathione / Q000378:metabolism*; D007700:Kinetics; D007774:Lactation; D008321:Mammary Glands, Animal / Q000378:metabolism*; D011247:Pregnancy; D051381:Rats; D013379:Substrate Specificity; D005723:gamma-Glutamyltransferase / Q000378:metabolism*
D000596:Amino Acids; D005723:gamma-Glutamyltransferase; D005978:Glutathione