Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
PROTEOLYSIS OF SPECIFIC MUSCLE STRUCTURAL PROTEINS BY MU-CALPAIN AT LOW PH AND TEMPERATURE IS SIMILAR TO DEGRADATION IN POSTMORTEM BOVINE MUSCLE
Autore:
HUFFLONERGAN E; MITSUHASHI T; BEEKMAN DD; PARRISH FC; OLSON DG; ROBSON RM;
Indirizzi:
IOWA STATE UNIV SCI & TECHNOL,DEPT ANIM SCI,MEAT LAB 214 AMES IA 50011 IOWA STATE UNIV SCI & TECHNOL,DEPT ANIM SCI,MEAT LAB 214 AMES IA 50011 IOWA STATE UNIV SCI & TECHNOL,DEPT BIOCHEM & BIOPHYS AMES IA 50011
Titolo Testata:
Journal of animal science
fascicolo: 5, volume: 74, anno: 1996,
pagine: 993 - 1008
SICI:
0021-8812(1996)74:5<993:POSMSP>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLYACRYLAMIDE GEL-ELECTROPHORESIS; CA++-DEPENDENT PROTEASES; CALCIUM ACTIVATED FACTOR; RABBIT SKELETAL-MUSCLE; MYOFIBRILLAR PROTEINS; IMMUNOELECTRON MICROSCOPY; MONOCLONAL-ANTIBODIES; CONNECTIN FILAMENTS; LONGISSIMUS MUSCLE; LYSOSOMAL-ENZYMES;
Keywords:
PROTEIN DEGRADATION; CALPAIN; BEEF; TENDERNESS; AGING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
61
Recensione:
Indirizzi per estratti:
Citazione:
E. Hufflonergan et al., "PROTEOLYSIS OF SPECIFIC MUSCLE STRUCTURAL PROTEINS BY MU-CALPAIN AT LOW PH AND TEMPERATURE IS SIMILAR TO DEGRADATION IN POSTMORTEM BOVINE MUSCLE", Journal of animal science, 74(5), 1996, pp. 993-1008

Abstract

Postmortem (PM) and mu-calpain-induced degradation of specific skeletal muscle proteins was monitored by SDS-PAGE and Western blotting. Samples were removed from bovine longissimus thoracis (LT) at approximately 45 min PM for the preparation of at-death (0-d) myofibrils (MF). The LT was excised at 1 d PM, vacuum-packaged, and stored at 2 degrees C. Samples were removed for Warner-Bratzler shear force analysis and biochemical analysis at 1, 3, 7, 14, 28, and 56 d PM. The protease mu-calpain was purified from bovine skeletal muscle and used to digest at-death MF at pH 5.6, 4 degrees C, 100 mu M CaCl2. Degradation of the proteins titin, nebulin, filamin, desmin, and troponin-T was monitored inthe PM and mu-calpain-digested samples by using SDS-PAGE and Western blotting. The PM samples that had significantly lower shear force (LSF) values (P <.05) at 1 d PM exhibited faster degradation of these fiveproteins than the higher shear force (HSF) samples. In LSF samples, the intact titin band (T1) was absent by 7 d PM and nebulin was absent by 3 d PM. In LSF samples, some filamin was degraded by 3 d PM, but inHSF samples degradation was not apparent until 14 d PM. In LSF samples, desmin was degraded more rapidly PM than in HSF samples. Troponin-Twas broken down PM to yield two major polypeptides of approximately 28 and 30 kDa; these polypeptides appeared earlier PM in LSF samples. Degradation products, similar to those observed PM, for all five proteins also were detected in Western blots of mu-calpain-digested MF, suggesting the calpain system plays a key role in PM protein degradation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 11:38:20