2005 年 55 巻 4 号 p. 315-321
Background : Myosin light chain kinase (MLCK), a regulatory protein of smooth muscle contraction, not only catalyzes the phosphorylation of the myosin regulatory light chain (MLc 20) 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.
