Stabilization of myosin by ionic compounds as affected by F-actin

被引:5
|
作者
Hayashi, Kumiko [1 ]
Konno, Kunihiko [1 ]
机构
[1] Hokkaido Univ, Fac Fisheries Sci, Hakodate, Hokkaido 0418611, Japan
关键词
amino acid; myosin; sugar; suppression of denaturation; thermal denaturation;
D O I
10.1111/j.1444-2906.2006.01294.x
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
Suppressive effects of non-ionic (sorbitol, maltose, and trehalose) and ionic (Na-glutamate, Na-acetate, Na-sulfate, and ammonium sulfate) compounds on the thermal inactivation of myosin subframgent-1 (S-1) and myofibril Ca2+-ATPase were compared. All compounds suppressed S-1 denaturation. When myofibrils were used (at 0.1 M KCl), sugars and sugar alcohol (non-ionic compounds) suppressed denaturation similar to S-1, while Na-glutamate, Na-acetate, and Na-sulfate weakly suppressed them. Ammonium sulfate accelerated denaturation, but suppressed denaturation when heated in 2 M KCl, at which myosin lost protection by F-actin. It was thus concluded that ionic compounds affected the denaturation of myofibrils in two ways; suppression as established with S-1, and acceleration as a result of loss of protection by F-actin caused by increase in ionic strength.
引用
收藏
页码:1306 / 1312
页数:7
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