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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.
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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

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References

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