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Development and evaluation of a real-time PCR method for determining skeletal muscle fibre type composition in sheep

Published online by Cambridge University Press:  23 November 2017

K. M. Hemmings ,
T Parr ,
P. J. Buttery  and
J. M. Brameld
K. M. Hemmings*
Affiliation:
The University of Nottingham, Nottingham, United Kingdom
T Parr
Affiliation:
The University of Nottingham, Nottingham, United Kingdom
P. J. Buttery
Affiliation:
The University of Nottingham, Ningbo, China
J. M. Brameld
Affiliation:
The University of Nottingham, Nottingham, United Kingdom
*
Email:sbxkmh@nottingham.ac.uk
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Extract

Myosin is a major contractile protein in skeletal muscle and its different isoforms reflect differences in the properties of fibres, with the major fibre types being named according to the isoform of myosin heavy chain they contain. Four major adult genes encoding isoforms of myosin heavy chain (MHC I, IIA, IIX and IIB) have been identified in skeletal muscle from a variety of species (Pette & Staron, 2000), the expression of these is a characteristic of muscle fibres. Differences in the number, size and proportions of fibres are suggested to affect growth performance and meat quality (Maltin et al., 2003). Conventional myosin ATPase staining characterises individual muscle fibres as slow (MHC type I) or fast (MHC Type IIA, IIX, IIB) based on the activity of myosin ATPase. We previously demonstrated that anti-myosin isoform antibodies could be used to identify muscle fibre compsition by comparing to myosin ATPase staining (Sazili et al 2005). The aim of this study was to develop a quantitative PCR method for determining ovine skeletal muscle fibre composition, based upon the expression of different adult MHC isoform transcripts.

Type
Theatre Presentations
Information
Proceedings of the British Society of Animal Science , Volume 2008 , 2008 , pp. 47
Copyright
Copyright © The British Society of Animal Science 2008

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References

Maltin, C., Balcerzak, D., Tilley, R & Delday, M. (2003) Determinants of meat quality: Tenderness. Proceedings of the Nutrition Society, 62, 337–347.CrossRefGoogle ScholarPubMed
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Sazili, A.Q., Parr, T., Sensky, P.L., Jones, S.W., Bardsley, R.G., Buttery, P.J. (2005) The relationship between slow and fast myosin heavy chain content, calpastatin and meat tenderness in different ovine skeletal muscles. Meat Science, 69, 17–25 CrossRefGoogle ScholarPubMed
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