A phosphorylated light-chain component of myosin
نویسندگان
چکیده
منابع مشابه
Sites phosphorylated in myosin light chain in contracting smooth muscle.
Purified smooth muscle myosin light chain can be phosphorylated at multiple sites by myosin light chain kinase and protein kinase C. We have determined the sites phosphorylated on myosin light chain in intact bovine tracheal smooth muscle. Stimulation with 10 microM carbachol resulted in 66 +/- 5% monophosphorylated and 11 +/- 2% diphosphorylated myosin light chain after 1 min, and 47 +/- 4% mo...
متن کاملPhosphorylated Myosin Light Chain 2 (p-MLC2) as a Molecular Marker of Antemortem Coronary Artery Spasm
BACKGROUND It is not uncommon that only mild coronary artery stenosis is grossly revealed after a system autopsy. While coronary artery spasm (CAS) is the suspected mechanism of these deaths, no specific biomarker has been identified to suggest antemortem CAS. MATERIAL AND METHODS To evaluate the potential of using phosphorylated myosin light chain 2 (p-MLC2) as a diagnostic marker of antemorte...
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...
متن کاملMyosin light-chain kinase of smooth muscle stimulates myosin ATPase activity without phosphorylating myosin light chain.
Myosin light-chain kinase (MLCK) of smooth muscle is multifunctional, being composed of N-terminal actin-binding domain, central kinase domain, and C-terminal myosin-binding domain. The kinase domain is the best characterized; this domain activates the interaction of smooth-muscle myosin with actin by phosphorylating the myosin light chain. We have recently shown that the Met-1-Pro-41 sequence ...
متن کاملEffects of relaxin on rat uterine myosin light chain kinase activity and myosin light chain phosphorylation.
Isometrically suspended uteri from estrogen-primed rats were stimulated with prostaglandin F2 alpha and then exposed to relaxin. Relaxin-dependent decreases in the ratio of phosphorylated to total myosin light chains (MLC) and in MLC kinase activity, measured in the presence of 0.5 mg/ml of uterine myosin and the absence and presence of Ca2+-calmodulin (CaM), were observed. The time-course and ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1972
ISSN: 0306-3283
DOI: 10.1042/bj1280105p