Characterization of Recombinant Full-Length, Smooth-Muscle Myosin Light Chain Kinase

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概要

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• Background : Myosin light chain kinase (MLCK), a regulatory protein of smooth muscle contraction, not only catalyzes the phosphorylation of the myosin regulatory light chain (MLc20) but also binds to actin. Full-length MLCK has not yet been successfully expressed, in spite of using various expression systems. Material and Methods : cDNA of the bovine stomach MLCK (BsMLCK) was expressed using an E.coli expression system. Result : Recombinant BsMLCK was expressed in a soluble form and phosphorylated MLc20. It also demonstrated actin-binding and actin-bundling activities. Conclusion : Recombinant BsMLCK, with the properties known for MLCK, was quantifiably expressed and is the first step in analyzing the structure and function of MLCK.

• 2005-11-01

著者

• Kawano Kazufumi

  Department Of Molecular And Cellular Pharmacology Faculty Of Medicine Gunma University Graduate Scho

• Kawano Kazuhumi

  Department of Molecular and Cellular Pharmacology, Faculty of Medicine, Gunma University Graduate School of Medicine

関連論文

• Characterization of Recombinant Full-Length, Smooth-Muscle Myosin Light Chain Kinase

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