Identification of two forms of myosin light chain kinase in turkey gizzard

FEBS Letters

Hartshorne, David J.¹  Hinkins, Susan¹  Walsh, Michael P.²  Muguruma, Michio¹ 

[1] Muscle Biology Group, Departments of Biochemistry and Nutrition and Food Science, University of Arizona, Tucson, AZ 85721, USA;Department of Medical Biochemistry, University of Calgary, Calgary, Alberta T2N 1N4, Canada

关键词: Myosin kinase;    Phosphorylation;    Calmodulin;    Calcium;    Smooth muscle;    Regulation;    ATPγS;    adenosine 5′-O-(3-thiotriphosphate);    CTP;    cytidine 5′-triphosphate;    DTT;    dithiothreitol;    EGTA;    ethylene glycol bis (β-aminoethyl ether)N;    N;    N′;    N′-tetraacetic acid;    ITP;    inosine 5′-triphosphate;    MLCK;    myosin light chain kinase;    PAGE;    polyacrylamide gel electrophoresis;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(83)80138-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two forms of myosin light chain kinase from turkey gizzard are separable by ion-exchange chromatography. One is the well-characterized 13 000 M _r enzyme. Purification of the second form by affinity chromatography on calmodulin-Sepharose showed it to consist of two polypeptide chains of M _r 136 000 and 141 000. This form of the enzyme required Ca²⁺ and calmodulin for activity, was specific for the M _r 20 000 light chain of myosin, and appeared to phosphorylate the same site on the light chain as the M _r 130 000 enzyme. The low-M _r gizzard kinase may be a proteolytic fragment of a higher-M _r species or these may represent different isoenzymes.

【 授权许可】

Unknown