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Intestinal absorption of amino acid derivatives: Structural requirements for membrane hydrolysis

✍ Scribed by G. L. Amidon; M. Lee; H. Lee

Publisher
John Wiley and Sons
Year
1983
Tongue
English
Weight
220 KB
Volume
72
Category
Article
ISSN
0022-3549

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✦ Synopsis

The intestinal absorption of L-lysine-p-nitroanilide, L-alanine-p-nitroanilide, and glycine-p-nitroanilide was studied in perfused rat intestine in the presence of a variety of potential competitive inhibitors. The results indicate that the hydrolysis site(s) show side-chain specificity, and that inhibitors require a free amino group in the alpha-position and must be in the L-configuration to be effective. Glycyl-L-proline, a peptide transport inhibitor, had no effect on the absorption rate.

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