Site of intestinal dipeptide hydrolysis.

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Abstract
Sacs of everted small intestine of hamsters were used to study the site of final hydrolysis of 12 dipeptides. L-alanyl-glycine, glycyl-glycine, L-valyl-L-valine, L-alanyl-L-valine, L-valyl-L-alanine and L-prolyl-glycine are apparently hydrolyzed beyond the locus of the active transport mechanism for D-glucose, perhaps even within the cell. These may be designated class 1 (deep) dipeptides. In contrast, superficial (perhaps even surface) hydrolysis seems to occur with L-alanyl-L-alanine, L-leucyl-L-leucine, glycyl-L-alanine, L-alanyl-L-leucine, L-leucyl-L-alanine and glycyl-L-proline. These may be designated class 2 (superficial) dipeptides. All the dipeptides were able to partially inhibit D-glucose active transport, the findings supporting the view that more than 1 mechanism may exist for the active absorption of the sugar.