Woodgett J R, Tonks N K, Cohen P
FEBS Lett. 1982 Nov 1;148(1):5-11. doi: 10.1016/0014-5793(82)81231-3.
A glycogen synthase kinase that is completely dependent on Ca2+ and calmodulin has been identified in mammalian skeletal muscle, and purified approximately 3000-fold by chromatography on phosphocellulose and calmodulin--Sepharose. The presence of 50 mM NaCl in the homogenisation buffer was critical for extraction of the enzyme. The calmodulin-dependent glycogen synthase kinase (app. Mr 850 000) is distinct from myosin light-chain kinase and phosphorylase kinase, but phosphorylates the same serine residue on glycogen synthase as phosphorylase kinase. The physiological role of the enzyme is discussed.
在哺乳动物骨骼肌中已鉴定出一种完全依赖钙离子和钙调蛋白的糖原合酶激酶,并通过磷酸纤维素和钙调蛋白-琼脂糖凝胶层析将其纯化了约3000倍。匀浆缓冲液中50 mM氯化钠的存在对该酶的提取至关重要。钙调蛋白依赖性糖原合酶激酶(表观分子量850 000)不同于肌球蛋白轻链激酶和磷酸化酶激酶,但与磷酸化酶激酶一样,能使糖原合酶上的同一位丝氨酸残基磷酸化。文中讨论了该酶的生理作用。