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 Kretchmar, D. H.
Right arrow Articles by Dayton, W. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kretchmar, D. H.
Right arrow Articles by Dayton, W. R.

Journal of Animal Science, Vol 68, Issue 6 1760-1772, Copyright © 1990 by American Society of Animal Science


JOURNAL ARTICLE

Alterations in postmortem degradation of myofibrillar proteins in muscle of lambs fed a beta-adrenergic agonist

D. H. Kretchmar, M. R. Hathaway, R. J. Epley and W. R. Dayton
Dept. of Anim. Sci., University of Minnesota, St. Paul 55108.

Dietary administration of 4 ppm of the beta-agonist L-644,969 (Merck Sharpe and Dohme Research Laboratories) to finishing lambs induced a decrease (10 to 14%, P less than .05) in extractable calpain I activity in the longissimus muscle (LD) at death (d 0). At 4 d postmortem (d 4), extractable calpain I levels in the LD of both control and treated lambs were reduced (P less than .001) from those present at d 0, but the extractable activity in the LD was reduced to a greater extent in control than in treated lambs. Calpain II activity was increased 42% (P less than .005) in LD of treated lambs; however, no significant differences were observed between d 0 and d 4 calpain II activity within treated or control LD samples (P greater than .1). Calpastatin activity was higher in the LD of treated lambs (74% on d 0, P less than .001 and 430% on d 4, P less than .001) than in the LD of control lambs. Measurable cathepsin B activity was decreased (29% on d 0, P less than .05) and measurable cathepsin H activity was increased (10% on d 0, P less than .05 and 10% on d 4, P less than .05) in the LD of treated lambs compared with controls. On d 2, 4 and 6 postmortem, degradation in myofibrils isolated from the LD was lower for treated than for control lambs. Warner-Bratzler shear values for loin chops from treated lambs were higher on both d 3 (111%) and 6 (108%) postmortem than for chops from control lambs (P less than .001). L-644,969-induced decreases in muscle proteolytic capacity may limit postmortem myofibril degradation and contribute to the reduced tenderness observed. This decreased proteolytic capacity may contribute to increased muscularity of L-644,969-treated lambs.


This article has been cited by other articles:


Home page
J ANIM SCIHome page
D. E. Goll, G. Neti, S. W. Mares, and V. F. Thompson
Myofibrillar protein turnover: The proteasome and the calpains
J Anim Sci, April 1, 2008; 86(14_suppl): E19 - E35.
[Abstract] [Full Text] [PDF]


Home page
J ANIM SCIHome page
G. H. Geesink, S. Kuchay, A. H. Chishti, and M. Koohmaraie
{micro}-Calpain is essential for postmortem proteolysis of muscle proteins
J Anim Sci, October 1, 2006; 84(10): 2834 - 2840.
[Abstract] [Full Text] [PDF]


Home page
J ANIM SCIHome page
M. P. Kent, M. J. Spencer, and M. Koohmaraie
Postmortem proteolysis is reduced in transgenic mice overexpressing calpastatin
J Anim Sci, March 1, 2004; 82(3): 794 - 801.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Cong, V. F. Thompson, D. E. Goll, and P. B. Antin
The Bovine Calpastatin Gene Promoter and a New N-terminal Region of the Protein Are Targets for cAMP-dependent Protein Kinase Activity
J. Biol. Chem., January 2, 1998; 273(1): 660 - 666.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1990 by the American Society of Animal Science.