Sato M, Ye L H, Kohama K
Department of Pharmacology, Gunma University School of Medicine.
J Biochem. 1995 Jul;118(1):1-3. doi: 10.1093/oxfordjournals.jbchem.a124862.
Myosin light chain kinase (MLCK) was prepared from smooth muscle of bovine aorta. MLCK inhibited the ATP-dependent movement of actin filaments on a glass surface coated with smooth muscle myosin that had been phosphorylated. The inhibitory effect was abolished by calmodulin in the presence of Ca2+ (Ca-CaM). The abolition was also observed when the concentration of actin filaments was increased. The inhibitory effect and its abolition were related to the actin-binding activity of MLCK, that is antagonized by Ca-CaM.
肌球蛋白轻链激酶（MLCK）是从牛主动脉平滑肌中制备的。MLCK抑制了肌动蛋白丝在涂有已磷酸化的平滑肌肌球蛋白的玻璃表面上依赖ATP的移动。在Ca2+（钙-钙调蛋白，Ca-CaM）存在的情况下，钙调蛋白消除了这种抑制作用。当肌动蛋白丝的浓度增加时，也观察到了这种消除现象。这种抑制作用及其消除与MLCK的肌动蛋白结合活性有关，而Ca-CaM可拮抗该活性。
