The intestinal absorption of fructosylglycine L leucine
Date of Original Version
The importance of free α amino groups in the hydrolysis and absorption of peptide bound amino acids has been studied in connection with the Maillard reaction of glycyl L leucine. The reaction of this dipeptide with an excess of glucose in methanol gave mostly a Maillard compound which appeared to be N,N di(1 deoxy 2 ketosyl) glycyl L leucine. In vitro, the Maillard product did not serve as a substrate for leucine aminopeptidase. Instead hydrolysis of normal glycylleucine was no longer observed when the Maillard compound was added in a 2:5 molar ratio. In vivo, the intact compound or its amino acid constituents were unabsorbed from the intestine of duodenum/portal vein cannulated rats, indicating that the residue adjacent to the N terminal amino acid of this Maillard dipeptide was not released by hydrolysis and transported because of its proximity to a Maillard reacted amino acid. The simultaneous presence of Maillard dipeptide did not appear to preclude or inhibit the absorption of normal glycyl L leucine.
Publication Title, e.g., Journal
Nutrition Reports International
Amaya-F., Jaime, T. C. Lee, and C. O. Chichester. "The intestinal absorption of fructosylglycine L leucine." Nutrition Reports International 14, 2 (1976): 229-235. https://digitalcommons.uri.edu/bps_facpubs/250