Myosin heavy chain composition of a large number (288) of single fibres from slow (soleus), and fast (superficial part of tibialis anterior, and plantaris) muscles of adult (3-5-month-old) Wistar rats was determined. A combination of SDS--PAGE and monoclonal antibodies against myosin heavy chains al
Co-existence of myosin heavy chain I and IIa isoforms in human skeletal muscle fibres with endurance training
✍ Scribed by H. Klitgaard; O. Bergman; R. Betto; G. Salviati; S. Schiaffino; T. Clausen; B. Saltin
- Publisher
- Springer
- Year
- 1990
- Tongue
- English
- Weight
- 494 KB
- Volume
- 416
- Category
- Article
- ISSN
- 0031-6768
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✦ Synopsis
The myosin heavy chain (MHC) composition of slng~ibres frc~nm, vastus lateralis was analysed by one-dimensional electrophoresis and immunoblottinq in three groups of young men with distinct difference in physical activity patterns. No major co-existence of MHC isoforms was found in the group with some daily physical activity. In the very sedentary group, however, 19±5% (P,0.05) of the fibres exhibited coexistence of F~C type IIa and IIb. Further, in the endurance trained group co-existence of M~C type I and IIa was manifested in 36±4% (p~0.05) of the fibres. Disuse and extreme usage of muscle both give rise to an elevation in co-expression of MHC isoforms in single muscle fibres but of markedly different combination of isoforms.
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