title: Site of intestinal dipeptide hydrolysis.
abstract: 1. Sacs of everted small intestine of the hamster have been used to study the site of final hydrolysis of twelve dipeptides. 2. The results suggest that L-alanyl-glycine, glycyl-glycine, L-valyl-L-valine, L-alanyl-L-valine, L-valyl-L-alanine and L-prolyl-glycine are hydrolysed beyond the locus of the active transport mechanism for D-glucose, perhaps even within the cell. These may be designated class 1 (deep) dipeptides. 3. In contrast, superficial (perhaps even surface) hydrolysis seems to occur with L-alanyl-L-alanine, L-leucly-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. 4. All the dipeptides were able to partially inhibit D-glucose active transport, the findings supporting the view that more than one mechanism may exist for the active absorption of the sugar.
mesh_terms: D000818:Animals; D001693:Biological Transport, Active / Q000187:drug effects; D006224:Cricetinae; D004151:Dipeptides / Q000378:metabolism* / Q000494:pharmacology; D005947:Glucose / Q000378:metabolism; D006868:Hydrolysis; D066298:In Vitro Techniques; D007408:Intestinal Absorption / Q000187:drug effects; D007421:Intestine, Small / Q000378:metabolism*
chemical_list: D004151:Dipeptides; D005947:Glucose