Cloning, Characterization and Bacterial Expression of the Physarum Myosin Light Chain kinase and Phosphorylatable Light Chain cDNAs.
نویسندگان
چکیده
منابع مشابه
Myosin light chain kinase structure function analysis using bacterial expression.
A 40-kDa fragment of chicken smooth muscle myosin light chain kinase was produced and partially purified from a bacterial expression system. This fragment exhibits calmodulin binding and substrate phosphorylation properties similar to those of the isolated chicken gizzard enzyme. A series of 3'-deletion mutants was prepared and used to produce proteins with the same NH2 terminus but with COOH t...
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Smooth muscle myosin light chain kinase was purified from turkey gizzards. The enzyme was extracted from washed myofibrils and the final step of purification was affinity chromatography using calmodulin coupled to Sepharose 4B. The purified enzyme was characterized with respect to its physical, chemical, and kinetic properties. It has a molecular weight of 130,000 by sodium dodecyl sulfate poly...
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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 ...
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 کاملDictyostelium discoideum myosin: isolation and characterization of cDNAs encoding the regulatory light chain.
Phosphorylation of the regulatory light chains (RMLC) of nonmuscle myosin can increase the actin-activated ATPase activity and filament formation. Little is known about these regulatory mechanisms and how the RMLC are involved in ATP hydrolysis. To better characterize the nonmuscle RMLC, we isolated cDNAs encoding the Dictyostelium RMLC. Using an antibody specific for the RMLC, we screened a la...
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ژورنال
عنوان ژورنال: Japanese Journal of Pharmacology
سال: 1996
ISSN: 0021-5198
DOI: 10.1016/s0021-5198(19)36705-8