The peptide, N-benzoyl-L-tyrosyl-p-aminobenzoic acid, which is used in an oral test of pancreatic function, has been perfused through isolated rat small intestine in order to determine whether it can be absorbed across the intestine in intact form, and whether it is hydrolysed appreciably by intestinal enzymes. For comparison, transport of N-benzoyl-DL-tyrosine, L-tyrosine, L-tyrosyl-L-leucine and p-aminobenzoic acid has also been studied. Very small amounts of bound tyrosine (probably mainly intact peptide plus some benzoyl-tyrosine) and of free p-aminobenzoic acid crossed the intestine during perfusion with N-benzoyl-L-tyrosyl-p-aminobenzoic acid. Adsorbed pancreatic enzymes were possibly responsible for the very small amount of hydrolysis of the peptide. However, no detectable free tyrosine crossed the intestine during perfusion with N-benzoyl-L-tyrosyl-p-aminobenzoic acid or with N-benzoyl-DL-tyrosine. In contrast, substantial quantities of free tyrosine crossed the intestine during perfusion with L-tyrosine or with L-tyrosyl-L-leucine. Net transport of tyrosine from L-tyrosyl-L-leucine was less than that from equimolar free L-tyrosine; no detectable intact L-tyrosyl-L-leucine crossed the intestine. During perfusion with free p-aminobenzoic acid the concentration in the serosal secretion apparently exceeded that in the lumen by a factor of 1.7; this suggests active transport of p-aminobenzoic acid.