Hostname: page-component-848d4c4894-wzw2p Total loading time: 0 Render date: 2024-05-05T13:06:19.468Z Has data issue: false hasContentIssue false
  • English
  • Français

Relationship between calpastatin activity and the slow and fast myosin heavy chain content of ovine skeletal muscles

Published online by Cambridge University Press:  20 November 2017

A.Q. Sazili ,
P.L. Sensky ,
T. Parr ,
R.G. Bardsley  and
P.J. Buttery
A.Q. Sazili
Affiliation:
Division of Nutritional Biochemistry, School of Biosciences, University of Nottingham, Sutton Bonington Campus, Loughborough, LE12 5RD, U.K.
P.L. Sensky
Affiliation:
Division of Nutritional Biochemistry, School of Biosciences, University of Nottingham, Sutton Bonington Campus, Loughborough, LE12 5RD, U.K.
T. Parr
Affiliation:
Division of Nutritional Biochemistry, School of Biosciences, University of Nottingham, Sutton Bonington Campus, Loughborough, LE12 5RD, U.K.
R.G. Bardsley
Affiliation:
Division of Nutritional Biochemistry, School of Biosciences, University of Nottingham, Sutton Bonington Campus, Loughborough, LE12 5RD, U.K.
P.J. Buttery
Affiliation:
Division of Nutritional Biochemistry, School of Biosciences, University of Nottingham, Sutton Bonington Campus, Loughborough, LE12 5RD, U.K.
Get access

Extract

Calpastatin, the specific endogenous inhibitor of the calpain system, is considered to be a principle contributor to variations in meat tenderisation (Parr et al., 1999). Previous studies have suggested that the differences in calpastatin activity in different ovine skeletal muscles could be influenced by muscle metabolic and contractile characteristics according to myofibrillar ATPase activity (Ouali and Talmant, 1990). The type of myofibrillar ATPase activity is largely determined by the content of slow or fast myosin heavy chains (Rivero et al., 1999). The present study was designed to investigate the relationship between calpastatin inhibitory activity and slow myosin heavy chain (MHC-s) and fast myosin heavy chain (MHC-f) expression.

Type
Poster Presentations
Information
Proceedings of the British Society of Animal Science , Volume 2002 , 2002 , pp. 173
Copyright
Copyright © The British Society of Animal Science 2002

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Ouali, A. and Talmant, A. 1990. Calpains and calpastatin distribution in bovine, porcine and ovine skeletal muscles. Meat Science 28: 331–348 Google Scholar
Parr, T., Sensky, P.L., Scothern, G.P., Bardsley, R.G., Buttery, P.J., Wood, J.D. and Warkup, C. 1999. Immunochemical study of the calpain system in porcine longissimus muscle with high and low shear force values. Journal of Animal Science 77 (suppl.1):164 Google Scholar
Sensky, P.L., Parr, T., Bardsley, R.G. and Buttery, P.J. 1996. The relationship between plasma epinephrine concentration and the activity of the calpain enzyme system in porcine longissimus muscle. Journal of Animal Science 74: 380–387 CrossRefGoogle ScholarPubMed
Singh, K., Dobbie, P.M., Simmons, N.J., Duganzich, D. and Bass, J.J. 1997. The effects of the calpain proteolytic system on meat tenderisation rates in different ovine skeletal muscles. Proceedings of the 43rd International Congress of Meat Science and Technology, New Zealand: 612–613 Google Scholar
Rivero, J.L.L., Talmadge, R.J. and Edgerton, V.R. 1999. Interrelationships of myofibrillar ATPase activity and metabolic properties of myosin heavy chain-based fibre types in rat skeletal muscle. Histochemistry and Cell Biology. 111: 277–287 Google Scholar