J. Anim Sci.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Boles, J. A.
Right arrow Articles by Robson, R. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Boles, J. A.
Right arrow Articles by Robson, R. M.

Journal of Animal Science, Vol 70, Issue 2 454-464, Copyright © 1992 by American Society of Animal Science


JOURNAL ARTICLE

Effect of porcine stress syndrome on the solubility and degradation of myofibrillar/cytoskeletal proteins

J. A. Boles, F. C. Parrish Jr, T. W. Huiatt and R. M. Robson
Department of Animal Science, Iowa State University, Ames 50011.

This study examined the effect of stress classification (stress-positive, stress-carrier, stress-negative) of pigs on selected properties of postmortem muscle, including protein solubility and degradation of proteins such as titin. Longissimus muscle samples were removed 45 min postslaughter, divided into samples, and stored at 0 to 2 degrees C for analysis at 0, 1, 3, 5, and 7 d postmortem. Whole-muscle samples (homogenates) and purified myofibrils were prepared from each sample for analysis by SDS-PAGE. A portion of each muscle sample also was extracted 1) with a low-ionic-strength solution to obtain a sarcoplasmic protein fraction and 2) with two different high-ionic-strength solutions to obtain a myofibrillar/cytoskeletal protein fraction for measurement of protein solubility and for analysis of extracts by SDS-PAGE. No significant differences were observed between muscle from stress-negative and stress-carrier animals in this study. Sarcoplasmic (P less than .05) and myofibrillar/cytoskeletal (P less than .01) protein solubility was lower in muscle samples from stress-positive animals than in muscle samples from stress-carrier and stress-negative animals at all postmortem times studied. The high molecular weight protein titin was degraded more slowly postmortem in muscle from stress-positive than in muscle from stress-negative animals, as observed by SDS-PAGE analysis of whole-muscle samples (homogenates) an myofibrils. The combination of lowered protein solubility and reduced rate of postmortem degradation of structural proteins such as titin may explain, at least in part, the reduced quality and protein functionality of muscle from stress-positive pigs.


This article has been cited by other articles:


Home page
Poult. Sci.Home page
C. Molette, V. Serieye, M. Rossignol, R. Babile, X. Fernandez, and H. Remignon
High Postmortem Temperature in Muscle Has Very Similar Consequences in Two Turkey Genetic Lines
Poult. Sci., December 1, 2006; 85(12): 2270 - 2277.
[Abstract] [Full Text] [PDF]


Home page
J ANIM SCIHome page
J. K. Apple, E. B. Kegley, C. V. Maxwell Jr., L. K. Rakes, D. Galloway, and T. J. Wistuba
Effects of dietary magnesium and short-duration transportation on stress response, postmortem muscle metabolism, and meat quality of finishing swine
J Anim Sci, July 1, 2005; 83(7): 1633 - 1645.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1992 by the American Society of Animal Science.