Myosin light chain kinase (MLCK) of smooth muscle stimulates myosin ATPase activity without phosphorylating myosin light chain.

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Myosin 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 ...

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Purification and characterization of smooth muscle myosin light chain kinase.

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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Myosin light chain kinase phosphorylation in tracheal smooth muscle.

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ژورنال

عنوان ژورنال: Japanese Journal of Pharmacology

سال: 1999

ISSN: 0021-5198

DOI: 10.1016/s0021-5198(19)35099-1