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 Geesink, G. H.
Right arrow Articles by Koohmaraie, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Geesink, G. H.
Right arrow Articles by Koohmaraie, M.

Journal of Animal Science, Vol 77, Issue 10 2685-2692, Copyright © 1999 by American Society of Animal Science

JOURNAL ARTICLE

Effect of calpastatin on degradation of myofibrillar proteins by mu-calpain under postmortem conditions

G. H. Geesink and M. Koohmaraie
Roman L. Hruska US Meat Animal Research Center, ARS, USDA, Clay Center, NE 68933-0166, USA.

To improve our understanding of the regulation of mu-calpain activity in situ during postmortem storage of muscle, the effect of different calpastatin levels on proteolysis of myofibrillar proteins by mu-calpain in a system closely mimicking postmortem conditions was studied. Increasing the amount of calpastatin in the incubations limited both the rate and extent of proteolysis of myofibrillar proteins and autolysis of mu-calpain. Excess calpastatin (i.e., a mu-calpain:calpastatin ratio of 1:4) did not inhibit proteolysis completely. Western blot analysis revealed that proteolysis of myofibrillar proteins virtually ceased after 7 d of incubation, despite the presence of partly autolyzed, therefore seemingly active, mu-calpain. A series of incubations of autolyzed mu-calpain revealed that the autolyzed form of this enzyme is unstable at an ionic strength observed in postmortem muscle. The possible significance of these results in terms of the regulation of mu-calpain activity in postmortem muscle is discussed.


This article has been cited by other articles:


Home page
 J ANIM SCIHome page
K. M. Carnagey, E. J. Huff-Lonergan, S. M. Lonergan, A. Trenkle, R. L. Horst, and D. C. Beitz
Use of 25-hydroxyvitamin D3 and dietary calcium to improve tenderness of beef from the round of beef cows
J Anim Sci, July 1, 2008; 86(7): 1637 - 1648.
[Abstract] [Full Text] [PDF]

Home page
 J ANIM SCIHome page
J. P. Camou, S. W. Mares, J. A. Marchello, R. Vazquez, M. Taylor, V. F. Thompson, and D. E. Goll
Isolation and characterization of {micro}-calpain, m-calpain, and calpastatin from postmortem muscle. I. Initial steps
J Anim Sci, December 1, 2007; 85(12): 3400 - 3414.
[Abstract] [Full Text] [PDF]

Home page
 J ANIM SCIHome page
J. P. Camou, J. A. Marchello, V. F. Thompson, S. W. Mares, and D. E. Goll
Effect of postmortem storage on activity of {micro}- and m-calpain in five bovine muscles
J Anim Sci, October 1, 2007; 85(10): 2670 - 2681.
[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
K. R. M. Carlin, E. Huff-Lonergan, L. J. Rowe, and S. M. Lonergan
Effect of oxidation, pH, and ionic strength on calpastatin inhibition of {micro}- and m-calpain
J Anim Sci, April 1, 2006; 84(4): 925 - 937.
[Abstract] [Full Text] [PDF]

Home page
 J ANIM SCIHome page
K. R. Maddock, E. Huff-Lonergan, L. J. Rowe, and S. M. Lonergan
Effect of pH and ionic strength on {micro}- and m-calpain inhibition by calpastatin
J Anim Sci, June 1, 2005; 83(6): 1370 - 1376.
[Abstract] [Full Text] [PDF]

Home page
 J ANIM SCIHome page
E. Veiseth, S. D. Shackelford, T. L. Wheeler, and M. Koohmaraie
Indicators of tenderization are detectable by 12 h postmortem in ovine longissimus
J Anim Sci, May 1, 2004; 82(5): 1428 - 1436.
[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
 Physiol. Rev.Home page
D. E. GOLL, V. F. THOMPSON, H. LI, W. WEI, and J. CONG
The Calpain System
Physiol Rev, July 1, 2003; 83(3): 731 - 801.
[Abstract] [Full Text] [PDF]

Home page
 J ANIM SCIHome page
B. T. Page, E. Casas, M. P. Heaton, N. G. Cullen, D. L. Hyndman, C. A. Morris, A. M. Crawford, T. L. Wheeler, M. Koohmaraie, J. W. Keele, et al.
Evaluation of single-nucleotide polymorphisms in CAPN1 for association with meat tenderness in cattle
J Anim Sci, December 1, 2002; 80(12): 3077 - 3085.
[Abstract] [Full Text] [PDF]

Home page
 J ANIM SCIHome page
L. Kristensen, M. Therkildsen, B. Riis, M. T. Sorensen, N. Oksbjerg, P. P. Purslow, and P. Ertbjerg
Dietary-induced changes of muscle growth rate in pigs: Effects on in vivo and postmortem muscle proteolysis and meat quality
J Anim Sci, November 1, 2002; 80(11): 2862 - 2871.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1999 by the American Society of Animal Science.