A Comparative Study of the Myosin Light Chain Kinases from Myoblast and Muscle Sources. Studies on the Kinases from Proliferative Rat Myoblasts in Culture, Rat Thigh muscle, and Rabbit Skeletal Muscle

Authors

S. P. Scordilis, Smith CollegeFollow
R. S. Adelstein, National Heart, Lung, and Blood Institute (NHLBI)

Document Type

Article

Publication Date

12-1-1978

Publication Title

Journal of Biological Chemistry

Abstract

Myosin light chain kinases have been isolated from rat thigh and rabbit skeletal muscle and cultured rat myoblasts. From these preparations, two types of kinases can be distinguished: calcium-dependent and calcium-independent. Both types of kinases can phosphorylate isolated P-light chains of myosin from several sources (skeletal muscle, cardiac muscle, and platelet). Data are shown which support the phosphorylation of the same site on the non-muscle P-light chains by both types of kinases. The rates of these reactions are, however, different for the two types of kinases. Kinetic analysis of the myoblast kinase show differing affinities for various P-light chains (non-muscle > cardiac > skeletal). In the proliferative rat myoblast, phosphorylation of myosin is a prerequisite for actin activation of the myosin ATPase activity.

Volume

253

Issue

24

First Page

9041

Last Page

9048

ISSN

00219258

Creative Commons License

This work is licensed under a Creative Commons Attribution 4.0 International License.

Comments

Archived as published. Open access article.

Recommended Citation

Scordilis, S. P. and Adelstein, R. S., "A Comparative Study of the Myosin Light Chain Kinases from Myoblast and Muscle Sources. Studies on the Kinases from Proliferative Rat Myoblasts in Culture, Rat Thigh muscle, and Rabbit Skeletal Muscle" (1978). Biological Sciences: Faculty Publications, Smith College, Northampton, MA.
https://scholarworks.smith.edu/bio_facpubs/141