THE BI-DIRECTIONAL REGULATION OF FILAMIN ON THE ATPase ACTIVITY OF MOOTH MUSCLE MYOSIN
- Author:
Yuan LIN
1
;
Huijun SUN
;
Shufang DAI
;
Zeyao TANG
;
Xin HE
;
Hua CHEN
Author Information
1. Dalian Medical University
- Keywords:
bi-directional regulation;
myosin binding;
myosin actin interaction
- From:
Chinese Medical Sciences Journal
2000;15(3):162-164
- CountryChina
- Language:Chinese
-
Abstract:
Objective. The aim of this study is to investigate the functional relationship between filamin, a known actin bind-ing protein, and myosin and the effects of filamin on the interaction between myosin and actin. Methods. Ultra-centrifugation method was used to investigate the binding of filamin to both phosphorylated and unphosphorylated myosins. Mg-ATPase activities of both phosphorylated and unphosphorylated myosins in the presence and absence of aefn were measured to observe the effects resulted from fdamin-actn and filamin-myosin interactions. Results. It was found that fiiamin is also a myosin binding protein. Filamin inhibited the actin activated Mg-ATPase activity of phosphorylated myosin and stimulated Mg-ATPase of phosphorylated myosin in the absence of actin;in addition, filamin stimulated Mg-ATPase activity of unphosphorylated myosin in both the presence or absence of actin.
