Immunoreactive levels of myosin light-chain kinase in normal and virus-transformed chicken embryo fibroblasts.
Open Access
- 1 October 1984
- journal article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 4 (10) , 2224-2226
- https://doi.org/10.1128/mcb.4.10.2224
Abstract
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.Keywords
This publication has 10 references indexed in Scilit:
- Biosynthesis of calmodulin in normal and virus-transformed chicken embryo fibroblasts.Molecular and Cellular Biology, 1984
- Substrate specificity of liver calmodulin-dependent glycogen synthase kinaseBiochemical and Biophysical Research Communications, 1983
- Phosphorylation of smooth muscle myosin light chain by five different kinasesFEBS Letters, 1983
- Analytical subcellular distribution of calmodulin and calmodulin-binding proteins in normal and virus-transformed fibroblasts.Journal of Biological Chemistry, 1983
- Regulatory Mechanisms in the Control of Protein KinaseCritical Reviews in Biochemistry, 1982
- [27] Purification of smooth muscle myosin light-chain kinasePublished by Elsevier ,1982
- Reproducible production of antiserum against vertebrate calmodulin and determination of the immunoreactive site.Journal of Biological Chemistry, 1981
- Human platelet myosin light chain kinase requires the calcium-binding protein calmodulin for activity.Proceedings of the National Academy of Sciences, 1979
- Composition of the myosin light chain kinase from chicken gizzardBiochemical and Biophysical Research Communications, 1977
- Calcium-dependent regulatory protein of cyclic nucleotide metabolism in normal and transformed chicken embryo fibroblasts.Proceedings of the National Academy of Sciences, 1976