首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >FORCE PRODUCTION BY CHEMICALLY CROSSLINKED MYOSIN-ACTIN CROSSBRIDGES IN RABBIT SKINNED FIBERS IN RESPONSE TO MGATP DEPLETION
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FORCE PRODUCTION BY CHEMICALLY CROSSLINKED MYOSIN-ACTIN CROSSBRIDGES IN RABBIT SKINNED FIBERS IN RESPONSE TO MGATP DEPLETION

机译:化学交联的肌球蛋白-肌动蛋白交联蛋白在兔皮纤维中的生产,以响应MGATP的消耗

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摘要

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. [References: 16]
机译:为了研究附着在细丝上的肌球蛋白横桥的收缩特性,在具有零长度化学交联剂1-(3-二甲基氨基-丙基)-3的单皮兔子腰大肌纤维中,将肌球蛋白头交联到其界面处的细丝上。 -乙基碳二亚胺(EDC)。获得的结果表明,当从肌原纤维空间中耗尽MgATP时,部分交联的单纤维会产生较大的严格样力。这种交联的纤维包含两种类型的交联的肌球蛋白头:一种是肌球蛋白分子的两个头之一与肌动蛋白交联,而另一头未交联。另一个具有与肌动蛋白交联的两个头。这项工作的结果表明,前一种类型的交联的肌球蛋白头部比后者具有更大的作用力。 [参考:16]

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