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
收藏
页码：742 / 746
页数：5
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