Evidence for Active Transport of the Dipeptide Carnosine (β-Alanyl-l-Histidine) by Hamster Jejunum in Vitro

1. The characteristics of intestinal transport and hydrolysis of carnosine (β-alanyl-l-histidine) have been studied in rings of everted hamster jejunum in vitro. 2. During incubation with carnosine, large amounts of intact peptide appeared in the intestinal wall, accompanied by small amounts of the constituent amino acids in the free form. Although there was some extracellular hydrolysis, the free amino acids appearing in the intestinal wall were almost entirely derived from intracellular hydrolysis of the peptide. Incubation in l-alanyl-l-histidine resulted in uptake of the constituent amino acids in the free form without appearance of intact peptide in the intestinal wall. 3. Total uptake of β-alanine (both peptide-bound and free) and total uptake of histidine were greater from a low concentration (1 μmol/ml) of carnosine than uptake of these amino acids from the equivalent amino acid mixture. At a high concentration of carnosine (20 μmol/ml), total uptake of β-alanine was greater from the peptide than from the equivalent amino acid mixture but total uptake of histidine was less. At this concentration, total uptake of β-alanine plus total uptake of histidine from the peptide was approximately the same as from the amino acid mixture. 4. Uptake of carnosine by jejunal rings was the result of a saturable process (Kt 9·4 μmol/ml, Vmax. 2·7 μmol g−1 initial wet wt. min−1). Intact carnosine was concentrated in the intestinal wall, the concentration ratio between intracellular fluid and incubation medium being up to 3·4/1. Uptake of carnosine was reduced by anoxia, metabolic inhibitors and replacement of medium Na+. Na+-dependent active transport was shown to be involved in uptake of carnosine by hamster jejunum in vitro.