Intestinal absorption of amino acid derivatives: structural requirements for membrane hydrolysis.
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.
D000409:Alanine / Q000378:metabolism; D000596:Amino Acids / Q000378:metabolism*; D000818:Animals; D005998:Glycine / Q000378:metabolism; D006868:Hydrolysis; D066298:In Vitro Techniques; D007408:Intestinal Absorption; D008239:Lysine / Q000378:metabolism; D008566:Membranes / Q000378:metabolism; D010477:Perfusion; D010539:Permeability; D051381:Rats; D013329:Structure-Activity Relationship
D000596:Amino Acids; D008239:Lysine; D000409:Alanine; D005998:Glycine