Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Effect of Postmortem Storage on Cold‐Shortened Bovine Muscle: Analysis by SDS‐Polyacrylamide Gel Electrophoresis

Effect of Postmortem Storage on Cold‐Shortened Bovine Muscle: Analysis by SDS‐Polyacrylamide Gel... ABSTRACT Myofibrils were isolated from the longissimus (L) muscle of control (CON) and cold‐shortened (CS) muscles after 0, 1, 3, 7, and 10 days of postmortem storage at 2°C. Isolated myofibrils were then examined by SDS‐polyacrylamide gel electrophoresis to monitor the changes in the myofibrillar proteins during postmortem storage. The main changes in CS muscles were the gradual appearance of 110,000‐, 95,000‐, and 30,000d‐dalton components and the disappearance of desmin and troponin‐T components of myofibrils. In addition, there was a gradual increase in the intensity of a protein around 55,000‐daltons. CON samples showed similar changes to those of CS samples. It appears that myofibrillar proteins of cold‐shortened muscles are affected by postmortem aging in a manner similar to that of the normally chilled muscles. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Food Science Wiley

Effect of Postmortem Storage on Cold‐Shortened Bovine Muscle: Analysis by SDS‐Polyacrylamide Gel Electrophoresis

Loading next page...
 
/lp/wiley/effect-of-postmortem-storage-on-cold-shortened-bovine-muscle-analysis-yz2VIOCcrS

References (23)

Publisher
Wiley
Copyright
Copyright © 1984 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-1147
eISSN
1750-3841
DOI
10.1111/j.1365-2621.1984.tb13731.x
Publisher site
See Article on Publisher Site

Abstract

ABSTRACT Myofibrils were isolated from the longissimus (L) muscle of control (CON) and cold‐shortened (CS) muscles after 0, 1, 3, 7, and 10 days of postmortem storage at 2°C. Isolated myofibrils were then examined by SDS‐polyacrylamide gel electrophoresis to monitor the changes in the myofibrillar proteins during postmortem storage. The main changes in CS muscles were the gradual appearance of 110,000‐, 95,000‐, and 30,000d‐dalton components and the disappearance of desmin and troponin‐T components of myofibrils. In addition, there was a gradual increase in the intensity of a protein around 55,000‐daltons. CON samples showed similar changes to those of CS samples. It appears that myofibrillar proteins of cold‐shortened muscles are affected by postmortem aging in a manner similar to that of the normally chilled muscles.

Journal

Journal of Food ScienceWiley

Published: Jan 1, 1984

There are no references for this article.