HEAT GELLING PROPERTIES OF MYOSIN, ACTIN, ACTOMYOSIN AND MYOSIN-SUBUNITS IN A SALINE MODEL SYSTEM

被引：129

作者：

SAMEJIMA, K

HASHIMOTO, Y

YASUI, T

FUKAZAWA, T

机构：

[1] The College of Dairy Agriculture, Ebetsu, Hokkaido, Nishinipporo

[2] Department of Animal Science, Faculty of Agriculture, Hokkaido University, Sapporo, Hokkaido

来源：

JOURNAL OF FOOD SCIENCE | 1969年 / 34卷 / 03期

关键词：

D O I：

10.1111/j.1365-2621.1969.tb10331.x

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

—Myosin and actin were isolated from rabbit skeletal muscle. The gelation of myosin, actin and actomyosin, as well as of heavy and light meromyosins derived from myosin by trypsin treatment, by heat was studied in various systems. The data indicate that the heat gelling properties of these protein solutions do not run parallel with those of saline model systems composed of these proteins and stroma. Actin does not exert any influence on the binding properties of the system, but when F‐actin and myosin A were both present the resulting binding properties were considerably improved. Since heavy and light meromyosins have little influence on binding properties, it may be concluded that an intact molecule of myosin is required for development of binding properties upon heating. Copyright © 1969, Wiley Blackwell. All rights reserved

引用

页码：242 / +

页数：1

共 24 条

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BARANY M, 1959, SULFUR PROTEINS, P321

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