Iwasa T, Inoue N, Miyamoto E
J Biochem. 1985 Aug;98(2):577-80. doi: 10.1093/oxfordjournals.jbchem.a135313.
A multifunctional calmodulin-dependent protein kinase in the canine cardiac cytosol was purified to near homogeneity. The purified enzyme inactivated glycogen synthase by means of phosphorylation. The enzyme also phosphorylated phospholamban and several other proteins. In view of its physicochemical properties and substrate specificity, the enzyme differed from myosin light chain kinase and phosphorylase kinase, and was considered to belong to a class of similar calmodulin-dependent protein kinases from brain, liver, and skeletal muscle. The results suggest that the enzyme mediates multiple Ca2+-dependent functions in the heart.
犬心肌细胞质中的一种多功能钙调蛋白依赖性蛋白激酶被纯化至近乎同质。纯化后的酶通过磷酸化作用使糖原合酶失活。该酶还能使受磷蛋白和其他几种蛋白质磷酸化。鉴于其理化性质和底物特异性,该酶不同于肌球蛋白轻链激酶和磷酸化酶激酶,被认为属于一类来自脑、肝和骨骼肌的类似钙调蛋白依赖性蛋白激酶。结果表明,该酶在心脏中介导多种钙依赖性功能。