Myosin filament depolymerizes in a low ionic strength solution containing L-histidine

被引：43

作者：

Hayakawa, T. ^{[1
]}

Ito, T. ^{[2
]}

Wakamatsu, J. ^{[1
]}

Nishimura, T. ^{[1
]}

Hattori, A. ^{[1
]}

机构：

[1] Hokkaido Univ, Meat Sci Lab, Grad Sch Agr, Kita Ku, Sapporo, Hokkaido 0608589, Japan

[2] Hokkaido Univ, Elect Microscope Lab, Grad Sch Agr, Kita Ku, Sapporo, Hokkaido 0608589, Japan

来源：

MEAT SCIENCE | 2010年 / 84卷 / 04期

基金：

日本学术振兴会;

关键词：

Myosin; L-histidine; Filament formation; Solubilization of protein; LIGHT-MEROMYOSIN; MUSCLE PROTEINS; SOLUBILITY; ROD;

D O I：

10.1016/j.meatsci.2009.11.010

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

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.

引用

页码：742 / 746

页数：5

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