Glutathione concentration and gamma-glutamyltransferase activity in water buffalo colostrum.

Evidence is presented that the buffalo mammary gland contains enzymes that catalyse the synthesis and utilization of glutathione. A significant, inverse correlation (r = 0.79) was detected between colostrum gamma-glutamyltransferase (GGT) and glutathione (GSH), suggesting that the enzyme uses GSH as a substrate for its activity. A similar trend was shown in mammary gland homogenates (r = 0.75). Our results show that GSH is secreted into buffalo colostrum and suggest that the enzyme GGT degrades it. To the authors' knowledge, this is the first demonstration of the involvement of GGT-mediated GSH metabolism in the synthesis of colostrums, which elucidates the role of the enzyme that has always been reported very high in colostrum.