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THERMAL-STABILITY OF FISH MYOSIN

被引：54
作者：
OGAWA, M
EHARA, T
TAMIYA, T
TSUCHIYA, T
机构：
[1] Department of Chemistry, Faculty of Science and Technology, Sophia University, 7-1, Kioi-cho, Chiyoda-ku, Tokyo 102, Japan
来源：
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1993年 / 106卷 / 03期
关键词：
D O I：
10.1016/0305-0491(93)90126-P
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
1. Thermal stability of fish myosin has been studied by using differential scanning calorimetry (DSC) and circular dichroism (CD). 2. The temperature range of the sharp decrease in alpha-helical content agreed very closely with that of the endothermic peaks. 3. There was a high correlation between the enthalpy of denaturation (DELTAH) and the decreasing quantity in alpha-helicity (DELTAh). 4. The structure of fish myosins was much more unstable than that of rabbit. 5. The instability of fish myosins was reflected in its rod moiety.
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页码：517 / 521
页数：5
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