| Autor: |
Reedy, M. K., Leonard, K. R., Freeman, R., Arad, T. |
| Zdroj: |
Journal of Muscle Research and Cell Motility; March 1981, Vol. 2 Issue: 1 p45-64, 20p |
| Abstrakt: |
An accurate value for mass/length of thick myofilaments is required to establish a limit for the maximum number of myosin molecules per crossbridge repeat. The mass/length of the crossbridge regions of desalted thick myofilaments from insect flight muscle (Lethocerus andMusca) and rabbit psoas has been measured with a computer-linked STEM by comparing the electron scattering signal per unit length of unstained thick filaments with that from TMV particles in the same image. Filament preparation was aided by limited digestion of myofibrils to remove Z bands using calcium-activated factor (CAF) from rabbit skeletal muscle; SDS gels showed that this selective protease spared myosin and tended to spare paramyosin but removed C protein.Lethocerus filaments prepared by the CAF procedure were 20–25% heavier per unit length than those prepared by conventional (simple) shearing, and retained a clear and generally uniform 14.5 nm crossbridge repeat by negative staining. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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