Dipeptide transport in isolated intestinal brush border membrane

Abstract

Transport of glycyl-L-leucine into isolated brush border membrane vesicles was studied. On the basis of the following observations it was postulated that glycyl-L-leucine was transported intact by a specific dipeptide mechanism. (1) The differing time course and Na-+ stimulation of glycine, L-leucine and glycyl-L-leucine. (2) The failure of glycine and L-leucine to inhibit glycyl-L-leucine transport. (3) Initial presence of dipeptide within the vesicle. (4) Inhibition of glycyl-L-leucine uptake by other dipeptides. (5) The occurrence of accelerated amino acid uptake in the presence of the dipeptide.