SUMMARY Intestinal perfusion studies performed in man have suggested that amino acid nitrogen may be absorbed more rapidly from peptides than free amino acids. The aim of the present study was to compare the effects of the oral administration of peptides and free amino acids. Two isonitrogenous liquid test meals, one containing 50 g of a partial enzymic hydrolysate of fish protein in which approximately 80 % of the nitrogen content was present as small peptides (peptide meal), and the other a mixture of free amino acids (amino acid meal) the composition and molar pattern of which simulated that of the peptide meal, were administered on separate occasions to six normal subjects intubated with a triple lumen tube. Both meals contained the reference marker polyethylene glycol. Fractional absorption of amino acid residues one and two hours after ingestion of the two meals was similar at three intestinal locations situated 120, 160, and 200 cm from the mouth of each subject, and at two hours 73-8 % and 72-0% of the amino acid residues had been absorbed respectively by the time the contents of the peptide and amino acid meals reached the middle sampling port of the tube. The total sum of individual amino acid increments in plasma was significantly greater 30 minutes (p < 0 025) and one hour (p < 005) after ingestion of the peptide than amino acid meals. By three hours the total area under the two plasma curves was similar. Normal human subjects thus appeared to be capable of assimilating orally administered mixtures of peptides and free amino acids with equal efficiency. Secretion of fluid into the lumen of the upper small intestine, assessed by reference to dilution of the polyethylene glycol, was less after ingestion of the peptide meal. In clinical situations characterised by fluid and electrolyte malabsorption consideration might be given to using small peptides rather than free amino acids as the nitrogen source in nutritional diets.The processes involved in the absorption of the final products of luminal proteolysis in the human small intestine are complex. Amino acids on release into free solution are absorbed by at least four group specific carrier-mediated active transport systems (Saunders and Isselbacher, 1966;Gray and Cooper, 1971). In addition to these transport systems, a separate system capable of mediating the transport of unhydrolysed dipeptides and tripeptides across the microvillous membrane into the mucosal cell has

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A B S T R A C T The mechanism of hydrolysis and absorption of a proline-containing tetrapeptide, Leu-ProGly-Gly (10 mM) by rat intestine was examined in vivo by using jejunal perfusion methods. The peptide substrate and hydrolysis products were analyzed by use of an automated amino acid analyzer. Leucine, proline, and glycine were absorbed by the intestine at a significantly higher rate from the tetrapeptide than from an equivalent amino acid mixture. The analysis of the hydrolytic products in the lumen during in vivo perfusion of the tetrapeptide showed that two dipeptides, Leu-Pro and Gly-Gly, were the major products. These two dipeptides were also the major hydrolytic products when a purified rat intestinal brush border membrane preparation was incubated with Leu-ProGly-Gly. The rate of hydrolysis of the tetrapeptide was much higher than that for several other proline-containing peptides (Leu-Pro, Pro-Leu, and Pro-Gly-Gly) that were tested. Studies using Gly-Pro-,B-naphthylamide, a specific substrate for postproline dipeptidyl aminopeptidase IV, showed that this enzyme is mainly localized to the brush border membrane and is responsible for the hydrolysis of the tetrapeptide into the two dipeptides Leu-Pro and Gly-Gly. Thus, brush border membrane dipeptidyl aminopeptidase IV very likely plays an important role at the intestinal mucosal cell surface in the final stages of digestion of prolinecontaining peptides.

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