Oligomerization of carp myosin which retains its ATPase activity

被引：15

作者：

Kato, S ^{[1
]}

Koseki, H ^{[1
]}

Konno, K ^{[1
]}

机构：

[1] HOKKAIDO UNIV,FAC FISHERIES,LAB FOOD BIOCHEM,HAKODATE,HOKKAIDO 041,JAPAN

来源：

FISHERIES SCIENCE | 1996年 / 62卷 / 06期

关键词：

fish myosin; thermal denaturation; oligomerization; aggregation; myosin filament;

D O I：

10.2331/fishsci.62.985

中图分类号：

S9 [水产、渔业];

学科分类号：

0908 ;

摘要：

Upon heating of carp myosin, actin-activated Mg-ATPase activity decreased much faster than its Ca-ATPase activity. Sepharose CL 4B gel filtration revealed that myosin formed oligomer, which retained its Ca-ATPase activity; oligomer at void volume (Vo) on Sepharose CL 4B exhibited ATPase activity. However, the Mg-ATPase/Ca-ATPase activity ratio for the Vo fraction was very low. Myosin filament formed by the oligomeric myosin at Vo was irregular. It was concluded that the low actin activated Mg-ATPase activity is responsible for the filament formed by oligomeric myosin. Oligomers were easily salted-out at 40% saturated ammonium sulfate, leaving monomers in the soluble fraction.

引用

页码：985 / 989

页数：5

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