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Titolo:
Matrix metalloproteinase activities of turkey (Meleagris gallopavo) bile
Autore:
Rath, NC; Huff, WE; Huff, GR; Balog, JM; Xie, H;
Indirizzi:
Univ Arkansas, Poultry Sci Ctr, USDA ARS, PPPSRU, Fayetteville, AR 72701 USA Univ Arkansas Fayetteville AR USA 72701 PPSRU, Fayetteville, AR 72701 USA
Titolo Testata:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY C-TOXICOLOGY & PHARMACOLOGY
fascicolo: 1, volume: 130, anno: 2001,
pagine: 97 - 105
SICI:
1532-0456(200109)130:1<97:MMAOT(>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
COLLAGENASE; EXPRESSION; GELATINASE; INHIBITORS; FIBROSIS; TISSUE; CELLS; PURIFICATION; INVASION; CHICKEN;
Keywords:
bile; collagenase; gelatinase; matrix metalloproteinase; thimerosal; turkeys; zymography;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Rath, NC Univ Arkansas, Poultry Sci Ctr, USDA ARS, PPPSRU, Fayetteville, AR 72701 USA Univ Arkansas Fayetteville AR USA 72701 yetteville, AR 72701 USA
Citazione:
N.C. Rath et al., "Matrix metalloproteinase activities of turkey (Meleagris gallopavo) bile", COMP BIOC C, 130(1), 2001, pp. 97-105

Abstract

The bile from turkey (Meleagris gallopavo) gall bladders was found to contain substantial matrix metalloproteinase (MMP) activities using gelatin, collagen, and casein substrate zymography, [H-3]labeled collagen degradation assays, and gelatin-agarose affinity purification. Five major bands corresponding to approximate M-w of 64, 60, 46, 40 and 36 kDa showed gelatinolyticactivities. On incubation with p-aminophenylmercuric acetate or thimerosal, the densities of both the 64- and 46-kDa bands decreased with increasing intensities of the 60- and 40-kDa bands. Both the 64- and 60-kDa bands showed collagenolytic activities whereas the caseinolytic activities appeared as diffuse bands corresponding to M-w of approximately 60, 40 and 36 kDa. Using [H-3]collagen as substrate, the bile enzymes showed both a time and concentration-de pendent degradation, which could be inhibited by the MMP inhibitors such as EDTA, phenanthroline, and N-[(2R)-2-(hydroxyamido carbonylmethyl)-4-methylpentanonyl]-L-tryptophan methylamide, but not by serine and cysteine protease inhibitors like trans-epoxysuccinyt-L-leucylamido-(4-guanidino)butane, phenylmethylsulfonyl fluoride or leupeptin. Both 60- and the 40-kDa. gelatinolytic bands showed affinity adsorption to a gelatin-agarose matrix. The physiological roles of bile MMPs are not clear, but their involvement in the digestive functions of birds are likely. (C) 2001 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 06:11:21