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- Edman, Anne-Christine, et al.
(author)
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Structural diversity in muscle fibres of chicken breast
- 1988
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In: Cell and Tissue Research. - 0302-766X .- 1432-0878. ; 251:2, s. 281-289
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Journal article (peer-reviewed)abstract
- hicken breast muscle is usually considered to be a relatively homogeneous white muscle and has therefore been widely used for studies of muscle proteins. In a previous study, however, we have found different M-region structures in different fibres from this muscle. Because of this result, we have now carried out a combined histochemical and ultrastructural survey of this muscle. In particular, we have made use of large transverse cryo-sections that include most of the muscle cross-section. Although the white region is fairly homogeneous in fibre content according to normal histochemical criteria (mATPase), we have found that there is a gradation of fibre structure across the muscle. The bulk of the muscle stains conventionally for Type-II fibres according to mATPase tests (the "white" part) but, in the small "red" part of the muscle, there are also Type-I fibres together with the Type-II fibres. Superimposed on this division into Type-I and Type-II fibres are variations in fibre size, oxidative and glycolytic staining properties, and variations of Z-band width and M-band structure; there is no strict correlation among any of these parameters. The apparently uniform staining across most of the muscle when tested for myofibrillar ATPase may be a misleading indicator of fibre properties.
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