Myosin is solubilized in a neutral and low ionic strength solution containing L-histidine

被引：73

作者：

Hayakawa, T. ^{[1
]}

Ito, T. ^{[2
]}

Wakamatsu, J. ^{[1
]}

Nishimura, T. ^{[1
]}

Hattori, A. ^{[1
]}

机构：

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

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

来源：

MEAT SCIENCE | 2009年 / 82卷 / 02期

关键词：

Myosin; Chicken breast muscle; Solubilization of protein; L-histidine; MUSCLE PROTEINS; ROD;

D O I：

10.1016/j.meatsci.2009.01.002

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, is insoluble at low and physiological ionic strength and soluble at high ionic strength. In this study, the behavior and morphology of myosin solubilized in a low ionic strength Solution containing L-histidine (L-His) was investigated. More than 80% of myosin was solubilized in a low ionic strength solution with dialysis against a solution containing 1 mM KCl and 5 MM L-His. Transmission electron microscopy with rotary shadowing demonstrated that the rod of myosin in a low ionic strength solution containing L-His is longer than that of myosin in a high ionic strength solution. The elongation of the myosin rod in a low ionic strength solution containing L-His would inhibit the formation of a filament, resulting in the solubilization of myosin. (c) 2009 Elsevier Ltd. All rights reserved.

引用

页码：151 / 154

页数：4

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