Open AccessImmunoreactive levels of myosin light-chain kinase in normal and virus-transformed chicken embryo fibroblasts.
Author(s) -
Linda J. Van Eldik,
Daniel Watterson,
Wilson H. Burgess
Publication year - 1984
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.4.10.2224
Subject(s) - myosin light chain kinase , calmodulin , biology , embryo , myosin , protein kinase a , calcium binding protein , kinase , microbiology and biotechnology , effector , immunoglobulin light chain , calcium , intracellular , binding protein , biochemistry , enzyme , antibody , gene , genetics , medicine
Calmodulin, a calcium-modulated effector protein, is an important mediator of the intracellular actions of calcium through its interaction with calmodulin-binding proteins. We report here that the immunoreactive levels of a calmodulin-binding protein, myosin light-chain kinase, are decreased in transformed chicken embryo fibroblasts.