A Ca2+‐sensitive actin regulatory protein from smooth muscle

FEBS Letters

Kanno, Kimiyoshi¹  Sasaki, Yasuharu¹  Hidaka, Hiroyoshi² 

[1] Biochemical Section, Technical Research Institute, Asahi Chemical Ind. Co., Asahi-machi 6-2700, Nobeoka 882, Japan;Department of Pharmacology, Mie University School of Medicine, Tsu 514, Japan

关键词: Actin polymerization Actin binding Gelsolin Ca2+ Bovine aorta Muscle;    DNase I;    pancreatic deoxyribonuclease I (EC 3.1.4.5);    PMSF;    phenylmethyl sulfonyl fluoride;   

DOI  :  10.1016/0014-5793(85)80607-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Using a procedure involving DNase I affinity chromatography and Sephadex G-200 gel filtration, we partially purified a Ca²⁺-sensitive actin regulatory 90-kDa protein from bovine aorta. The 90-kDa protein existed in the form of a complex with actin on a DNase I column even in the presence of 5 mM EGTA, indicating that the 90-kDa protein binds tightly to actin in a Ca²⁺-insensitive manner. The isolation procedure described above indicates that the 90-kDa protein is present in smooth muscles including aorta, uterus and bladder, but not in skeletal and heart muscles. When added to G-actin before polymerization, the 90-kDa protein increases the initial rate of actin polymerization and lowers the final viscosity at Ca²⁺ concentrations greater than 10⁻⁷M. This decrease in viscosity is due to the generation of filaments which cannot be readily sedimented.

【 授权许可】

Unknown