ArticleThe Biochemical journal1987
Purification, characterization and substrate specificity of calmodulin-dependent myosin light-chain kinase from bovine brain.
Article in The Biochemical journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 18 citations in OpenAlex.
- Stimulation of myosin light-chain kinase by Cd2+ and Pb2+.Archives of toxicology · 1995Article
- Molecular characterization of a mammalian smooth muscle myosin light chain kinase.The Journal of biological chemistry · 1991Article
- Phosphorylation of smooth muscle myosin by type II Ca2+/calmodulin-dependent protein kinase.Molecular and cellular biochemistry · 1990Article
- Purification and characterization of myosin light-chain kinase from the rat pancreas.The Biochemical journal · 1989Article
- Calmodulin-dependent multifunctional protein kinase in Aspergillus nidulans.Proceedings of the National Academy of Sciences of the United States of America · 1988Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A substrate-specific calmodulin-dependent myosin light-chain kinase (MLCK) was purified 45,000-fold to near homogeneity from bovine brain in 12% yield. Bovine brain MLCK phosphorylates a serine residue in the isolated turkey gizzard myosin light chain (MLC), with a specific activity of 1.8 mumol/min per mg of enzyme. The regulatory MLC present in intact gizzard myosin is also phosphorylated by the enzyme. The Mr-19,000 rabbit skeletal-muscle MLC is a substrate; however, the rate of its phosphorylation is at best 30% of that obtained with turkey gizzard MLC. Phosphorylation of all other protein substrates tested is less than 1% of that observed with gizzard MLC as substrate. SDS/polyacrylamide-gel electrophoresis of purified MLCK reveals the presence of a major protein band with an apparent Mr of 152000, which is capable of binding 125I-calmodulin in a Ca2+-dependent manner. Phosphorylation of MLCK by the catalytic subunit of cyclic-AMP-dependent protein kinase results in the incorporation of phosphate into the Mr-152,000 protein band and a marked decrease in the affinity of MLCK for calmodulin. The presence of Ca2+ and calmodulin inhibits the phosphorylation of the enzyme. Bovine brain MLCK appears similar to MLCKs isolated from platelets and various forms of muscle.
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