Myosin filament depolymerizes in a low ionic strength solution containing L-histidine
Myosin filament depolymerizes in a low ionic strength solution containing L-histidine
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DOI：
10.1016/j.meatsci.2009.11.010
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发表时间：
2010-04-01
期刊：
影响因子：
7.1
通讯作者：
Hattori, A.
中科院分区：
文献类型：
--
作者：
Hayakawa, T.;Ito, T.;Hattori, A.
肌球蛋白是一种主要的肌原纤维蛋白，形成丝状聚合物，不溶于生理和低离子强度溶液。我们已经表明，肌球蛋白是可溶于低离子强度的溶液中含有L-组氨酸。在这项研究中，以澄清的作用，L-组氨酸在肌球蛋白的增溶，我们研究了影响L-组氨酸的细丝形成和肌球蛋白的形态在低离子强度。在L-组氨酸存在下，肌球蛋白在生理离子强度溶液中形成丝状聚合物，并分散在低离子强度溶液中。透射电子显微镜显示，轻肌球蛋白（LMM），肌球蛋白的杆区域，在低离子强度溶液中含有L-组氨酸比在高离子强度溶液中没有L-组氨酸。L-组氨酸引起肌球蛋白LMM区的延长，有助于肌球蛋白丝的弱化和肌球蛋白在低离子强度溶液中的解离。(C)2009爱思唯尔有限公司保留所有权利。
Myosin, one of the major myofibrillar proteins, forms a filamentous polymer and is insoluble in physiological and low ionic strength solutions. We have shown that myosin is soluble in a low ionic strength solution containing L-histidine. In this study, to clarify the role of L-histidine in the solubilization of myosin, we investigated effects of L-histidine on the filament formation and the morphology of myosin at a low ionic strength. In the presence of L-histidine, myosin formed a filamentous polymer in a physiological ionic strength solution and dispersed in a low ionic strength solution. Transmission electron microscopy showed that light meromyosin (LMM), the rod region of myosin, in a low ionic strength solution containing L-histidine was longer than that in a high ionic strength solution without L-histidine. L-histidine causes the elongation of LMM region of myosin contributing to the weakening of the myosin filament and the dissociation of myosin in a low ionic strength solution. (C) 2009 Elsevier Ltd. All rights reserved.