Substrate specificity of myosin light chain kinases.
نویسندگان
چکیده
منابع مشابه
Phosphorylation of Mammalian Myosin Light Chain Kinases
The phosphorylation of the calmodulin-dependent enzyme myosin light chain kinase, purified from bovine tracheal smooth muscle and human blood platelets, by the catalytic subunit of CAMP-dependent protein kinase and by cGMP-dependent protein kinase was investigated. When myosin light chain kinase which has calmodulin bound is phosphorylated by the catalytic subunit of CAMP-dependent protein kina...
متن کاملPurification, characterization and substrate specificity of calmodulin-dependent myosin light-chain kinase from bovine brain.
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 ...
متن کاملStructural requirement of the regulatory light chain of smooth muscle myosin as a substrate for myosin light chain kinase.
The substrate structure required for skeletal and smooth muscle myosin light chain kinases (MLC kinase) was studied by using various mutant regulatory light chains of smooth muscle myosin. The deletion of the NH2-terminal 10 residues did not greatly affect the kinetic parameters of smooth MLC kinase; however, deletion of an additional 3 residues, Lys11-Arg13, prevented phosphorylation. In contr...
متن کاملAlterations in expression of myosin and myosin light chain kinases in response to vascular injury.
Histochemical analysis of balloon-injured rat carotid arteries revealed a coordinated expression of nonmuscle myosin heavy chain-A and -B (NM-A and NM-B) in response to injury. Expression of these nonmuscle myosin forms shifts from the media to the adventitia and intima. In contrast, expression of smooth muscle myosin heavy chain-1 (SM-1) within the media is not altered, whereas smooth muscle m...
متن کاملMyosin light-chain phosphatase.
1. A method for the isolation of a new enzyme, myosin light-chain phosphatase, from rabbit white skeletal muscle by using a Sepharose-phosphorylated myosin light-chain affinity column is described. 2. The enzyme migrated as a single component on electrophoresis in sodium dodecyl sulphate/polyacrylamide gel at pH7.0, with apparent mol.wt. 70000. 3. The enzyme was highly specific for the phosphor...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1992
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)35700-4