Abstract
Purified rabbit intestinal brush border membrane vesicles transport glycyl-L-proline into an osmotically responsive intravesicular space by a Na +- independent, carrier-mediated process. With short incubation, transport occurs mostly as the intact dipeptide, followed by hydrolysis. Pretreatment of the vesicles with papain results in a 60% reduction of L-alanine transport while glycyl-L-proline transport is stimulated by 40%. Papain treatment does not change the intravesicular volume, nor does it increase membrane permeability. Dipeptide transport into papain treated vesicles remains completely Na +- independent as it is in the control vesicles. Many dipeptides inhibit glycyl-L-proline transport into papain treated vesicles both in the presence and absence of a Na + gradient.
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