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Comparison of immunochemical and histochemical analysis of fibre type distribution in ovine skeletal muscles

Published online by Cambridge University Press:  20 November 2017

A. Q. Sazili
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.
P. L. Sensky
Affiliation:
Division of Nutritional Biochemistry, School of Biosciences, University of Nottingham, Sutton Bonington Campus, Loughborough, LE12 5RD, U.K.
S.W. Jones
Affiliation:
School of Biomedical Sciences, Queens Medical Centre, Nottingham, NG7 2UH.
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

The characterisation of muscle fibres has become increasingly important as the proportion of slow and fast fibre types are known to influence the biochemical and physiological properties of muscle during postmortem tenderisation (Ouali and Talmant, 1990). Current histochemical methods are labour intensive, time consuming and hazardous, requiring rapid freezing of samples in isopentane cooled in liquid nitrogen. The purpose of this study was to investigate an alternative immunochemical approach for identifying fibre types by examining the expression of slow myosin heavy chain (MHC-s) and fast myosin heavy chain (MHC-f) and comparing the data with classical histochemical techniques. Five different ovine skeletal muscles with known differences in fibre types distribution were studied.

Type
Poster Presentations
Copyright
Copyright © The British Society of Animal Science 2002

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References

Brooke, M.H. and Kaiser, K.K. 1970. Three “myosin ATPase” systems. The nature of their pH liability and sulphydryl dependence. Journal of Histochemistry and Cytochemistry. 18: 670672 Google Scholar
Ouali, A. and Talmant, A. 1990. Calpains and calpastatin distribution in bovine, porcine and ovine skeletal muscles. Meat Science 28: 331348 Google Scholar