Functional domain of caldesmon

FEBS Letters

Dąbrowska, Renata¹  Szpacenko, Adam¹ 

[1] Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, 3 Pasteur Str., 02-093 Warsaw, Poland

关键词: (Chicken gizzard);    Caldesmon;    Chymotryptic cleavage;    Functional domain;   

DOI  :  10.1016/0014-5793(86)80683-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Limted proteolysis of caldesmon has been used in studying the structure-function relationship of this protein. Digestion with α-chymotrypsin yields three major fragments of 110, 80 and 40 kDa. Only the 40 kDa fragment preserves functional properties of the parent molecule: it binds to F-actin, causes inhibition of actomyosin ATPase and binds to calmodulin in a Ca²⁺-dependent manner. Its further degradation produces an 18 kDa polypeptide that also retains all these properties. Neither F-actin nor calmodulin binding induces dramatic changes in susceptibility to chymotryptic cleavage and the sites of cleavage of caldesmon.

【 授权许可】

Unknown