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Site of intestinal dipeptide hydrolysis.
Author(s) -
Wiseman G
Publication year - 1977
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.1977.sp012120
Subject(s) - dipeptide , alanine , chemistry , hydrolysis , glycine , valine , leucine , stereochemistry , biochemistry , amino acid
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.