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

J Pharm Sci. 1983 Aug;72(8):943-4. doi: 10.1002/jps.2600720826.

Abstract

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alanine / metabolism
  • Amino Acids / metabolism*
  • Animals
  • Glycine / metabolism
  • Hydrolysis
  • In Vitro Techniques
  • Intestinal Absorption*
  • Lysine / metabolism
  • Membranes / metabolism
  • Perfusion
  • Permeability
  • Rats
  • Structure-Activity Relationship

Substances

  • Amino Acids
  • Lysine
  • Alanine
  • Glycine