Analysis of peptide metabolism by ruminal microorganisms.

R. J. Wallace, N. McKain

Research output: Contribution to journalArticle

51 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)2372-2376
Number of pages5
JournalApplied and Environmental Microbiology
Volume55
Issue number9
Publication statusPublished - Sep 1989

Fingerprint

rumen microorganisms
peptidases
Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
peptide
microorganism
metabolism
peptides
rumen fluids
substrate
Peptides
hydrolysis
Hydrolysis
fluid
reversed-phase liquid chromatography
Reverse-Phase Chromatography
Fluorescent Dyes
Chromatography
liquid chromatography
chromatography
Peptide Hydrolases

Cite this

Analysis of peptide metabolism by ruminal microorganisms. / Wallace, R. J.; McKain, N.

In: Applied and Environmental Microbiology, Vol. 55, No. 9, 09.1989, p. 2372-2376.

Research output: Contribution to journalArticle

@article{66e21a7c184f415fa50ef59ca60184ea,
title = "Analysis of peptide metabolism by ruminal microorganisms.",
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.",
author = "Wallace, {R. J.} and N. McKain",
note = "Medline is the source for the citation and abstract of this record.",
year = "1989",
month = "9",
language = "English",
volume = "55",
pages = "2372--2376",
journal = "Applied and Environmental Microbiology",
issn = "0099-2240",
publisher = "American Society for Microbiology",
number = "9",

}

TY - JOUR

T1 - Analysis of peptide metabolism by ruminal microorganisms.

AU - Wallace, R. J.

AU - McKain, N.

N1 - Medline is the source for the citation and abstract of this record.

PY - 1989/9

Y1 - 1989/9

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0024724301&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0024724301

VL - 55

SP - 2372

EP - 2376

JO - Applied and Environmental Microbiology

JF - Applied and Environmental Microbiology

SN - 0099-2240

IS - 9

ER -