Autor: |
Emoto, Yumiko, Tawada, Katsuhisa |
Zdroj: |
Biophysical Chemistry; October 1996, Vol. 61 Issue: 2-3 p85-92, 8p |
Abstrakt: |
In order to study the contractile property of myosin crossbridges attached to thin filaments, myosin heads were crosslinked to the filaments at their interface in single skinned rabbit psoas fibers with a zero-length chemical crosslinker, 1-(3-dimethylamino-propyl)-3-ethylcarbodiimide (EDC). The results obtained show that a partially crosslinked single fiber produces a large rigor-like force when MgATP is depleted from the myofibrillar space. Such crosslinked fibers contain two types of crosslinked myosin heads: one with one of the two heads of the myosin molecule crosslinked to actin with the other head uncrosslinked; the other has both heads crosslinked to actin. The results of this work suggest that a crosslinked myosin head of the former type produces a much larger force than the latter type. |
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