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Appl Environ Microbiol. 1989 September; 55(9): 2372-2376

Analysis of peptide metabolism by ruminal microorganisms.

Rowett Research Institute, Aberdeen, United Kingdom.

ABSTRACT

Methods were developed for the determination of oligoalanine and other short-chain peptides and peptide analogs in ruminal fluid by using reverse-phase high-pressure liquid chromatography. Chromatographic analysis of the breakdown of (Ala)3 and (Ala)4 in ruminal fluid in vitro revealed that the predominant mechanism of hydrolysis was a dipeptidyl peptidase-like activity. Hydrolysis proceeded from the N terminal of the peptide chain; N-acetyl-(Ala)3 was broken down at 11% of the rate of breakdown of (Ala)3 or (Ala)3-p-nitroanilide. (Ala)2-p-nitroanilide was hydrolyzed most rapidly of the arylamide substrates tested, but fluorogenic 4-methoxy-2-naphthylamide (MNA) compounds were more convenient and potentially more versatile substrates than p-nitroanilides. Gly-Arg-MNA was the most rapidly hydrolyzed dipeptidyl peptidase substrate, suggesting that ruminal peptidase activity was predominantly of a type I specificity.

This article has been cited by other articles:

• Walker, N. D., McEwan, N. R., Wallace, R. J. (2003). Cloning and functional expression of dipeptidyl peptidase IV from the ruminal bacterium Prevotella albensis M384T. Microbiology 149: 2227-2234 [Abstract] [Full Text]  
• Eschenlauer, S. C. P., McKain, N., Walker, N. D., McEwan, N. R., Newbold, C. J., Wallace, R. J. (2002). Ammonia Production by Ruminal Microorganisms and Enumeration, Isolation, and Characterization of Bacteria Capable of Growth on Peptides and Amino Acids from the Sheep Rumen. Appl. Environ. Microbiol. 68: 4925-4931 [Abstract] [Full Text]