Active site of intestinal gamma-glutamyltransferase faces luminal side of brush border membrane.

Abstract

Purified gamma-glutamyltransferase from hog small intestine was competitively inhibited by glutathione in vitro when L-gamma-glutamyl-p-nitroanilide was used as a substrate. An S-acetyldextran derivative of glutathione inhibited the enzyme as well as glutathione, although dextran had no inhibitory effect. gamma-Glutamyltransferase in the rat small intestine could utilize in situ L-gamma-glutamyl-p-nitroanilide circulated in the lumen, and was inhibited by the impermeable derivative of glutathione which was on the luminal side. These data suggested that the active site of intestinal gamma-glutamyltransferase faced the luminal side of the brush border membrane.