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Small quantities of low-molecular weight peptides have been characterized in the feces of axenic mice. In fecal material of axenic mice fed an autoclaved synthetic (SN) diet, we isolated a dipeptide and characterized its structure as beta-aspartyl-epsilon-lysine. This product was also present in the feces of gnotobiotic mice harbouring Clostridium perenne. We could not detect the product in the fecal contents of holoxenic mice, Clostridium difficile-contaminated mice or axenic mice fed the irradiated SN diet. The peptide, beta-aspartyl-epsilon-lysine, was produced by heating proteins during sterilization, causing the formation of a pseudopeptide bond between the epsilon-amino group of lysine and the amide group of asparagine. The intestinal strains seemed to differ in their ability to split this pseudopeptide bond in vivo.

In this study, we used fasted, preruminant calves fitted with a double proximal cannula in the duodenum; gastric evacuation was investigated by recovering products leaving the abomasum after a test meal. Five types of meal were given: whole milk, skimmed milk, casein solution in water, casein solution in a mineral medium simulating the permeate of highly-filtered milk, and whey. Gastric emptying of nitrogen was relatively slow. The coagulation of "milk diets" slowed down this emptying. Precipitation of "casein diets" at acid pH also slowed down emptying, but to a lesser degree. The "casein diets", more proteolyzed than the "milk diets", released larger amounts of non-protein nitrogen (NPN) into the intestine. Calcium emptying was highly related to NPN emptying, demonstrating the important role of acid peptides (phosphopeptides) from casein hydrolysis.

Gastric digestion of milk proteins has been studied in the preruminant calf by analysing gastric effluents in the duodenum after the ingestion of 5 different diets: whole milk, skim milk, casein solution in water, casein solution with minerals, whey. The amino acid composition of the gastric effluents and HPLC analysis of the latter show that the major part of the whey proteins were evacuated rapidly without any proteolysis and after milk ingestion. On the contrary, all the caseins were largely proteolysed and arrived slowly in the gut. The major part of the peptides obtained came from alpha s1 casein. Only a few peptides, principally CMP, were quickly emptied from the stomach.

Peptide products insoluble in 12% TCA and obtained in the proximal duodenum of calves at different times after ingestion of casein solutions were characterized by polyacrylamide gel electrophoresis, electrofocusing and SDS pore gradient gel electrophoresis. With a 3% whole-casein solution in water the disappearance of electrophoretic bands corresponding to alpha s1 and beta caseins was observed after about 1 h 30. After 3 h and up to 7 h very acidic peptides appeared. With a 3% whole-casein solution in simulated milk ultrafiltrate, comparable patterns were obtained. Nevertheless, the acidic peptides appeared sooner, i.e. they were already detected in the first sample collected after meal ingestion. With the 2 diets, the importance of gastric proteolysis was demonstrated by the appearance of a great number of peptides of various sizes, charges and pHi. On the other hand, an effect of salts on casein proteolysis was detected.

This review, written for non-specialists, describes briefly the steps of protein biosynthesis from their precursors in the blood to the excreted molecules, taking rat gamma-casein as an example. A schematic description is given of the procedures employed for preparing cDNAs which can provide the sequences of the corresponding mRNAs and proteins. Recent findings concerning milk proteins are briefly mentioned, and in particular those dealing with sequence determinations of mRNAs coding for milk proteins from several species.

Calves were fed five different test meals: whole milk, skim milk, 3% whole casein solution, 3% whole casein in simulated milk ultrafiltrate, and whey. The digesta leaving the abomasum before feeding and during the first 7 postprandial hours were collected by fractions. After precipitation with 12% TCA, the amino acid compositions of the sediments and the supernatants were determined and compared by multivariate analysis. The composition of prefeeding digesta was similar to that of gastric juice. When the calves were fed the two casein diets, the amino acid composition of the sediments changed little with time. In contrast, the changes observed in the composition of the supernatants suggested rapid abomasal emptying of caseino-macro peptide. With the whey diet, it was not possible to evidence more rapid hydrolysis or abomasal emptying of any particular whey protein. During the first 10 min following the ingestion of whole or skim milk, the amino acid composition of the sediment was close to that of milk protein. Immediately afterwards, the composition of the sediment was similar to that of whey protein. Thereafter, the composition of the sediment became more like that of casein and almost reached that of casein during the 7th hour. The amino acid composition of the supernatant was similar to that obtained with the casein diets; this fact suggests that the small peptides produced by proteolysis in the abomasum originated more from casein than from whey proteins.