Singh T J
Department of Biology, University of Waterloo, Ontario, Canada.
FEBS Lett. 1989 Jan 30;243(2):289-92. doi: 10.1016/0014-5793(89)80147-4.
Two casein kinases, casein kinase-1 (CK-1) and casein kinase-2 (CK-2), have been characterized from many sources. In this study we describe the properties of a third casein kinase, designated casein kinase-3 (CK-3). CK-3 (Mr 32,000) is readily separated from CK-2 by gel filtration and from CK-1 by hydroxyapatite chromatography. CK-3 phosphorylates several proteins, including phosphorylase kinase. Phosphorylation of phosphorylase kinase by CK-3 results in a 10-fold enzyme activation. CK-3 is activated by spermine and inhibited by heparin, ADP, and divalent metal ions (Mn2+, Zn2+). Heparin inhibition of the kinase is reversed by spermine. The physical and regulatory properties of CK-3 are very similar to CK-1, suggesting that these kinases may be closely related.
已经从多种来源鉴定出两种酪蛋白激酶，即酪蛋白激酶-1（CK-1）和酪蛋白激酶-2（CK-2）。在本研究中，我们描述了第三种酪蛋白激酶的特性，命名为酪蛋白激酶-3（CK-3）。CK-3（分子量32,000）通过凝胶过滤可轻松与CK-2分离，通过羟基磷灰石色谱可与CK-1分离。CK-3可磷酸化多种蛋白质，包括磷酸化酶激酶。CK-3对磷酸化酶激酶的磷酸化导致该酶活性增强10倍。CK-3被精胺激活，被肝素、ADP和二价金属离子（Mn2+、Zn2+）抑制。精胺可逆转肝素对该激酶的抑制作用。CK-3的物理和调节特性与CK-1非常相似，表明这些激酶可能密切相关。
