Grasser K D, Maier U G, Feix G
Institute for Biology III, Albert-Ludwigs-Universität, Freiburg, FRG.
Biochem Biophys Res Commun. 1989 Jul 14;162(1):456-63. doi: 10.1016/0006-291x(89)92019-6.
A casein kinase of the type II was isolated and enriched from nuclear lysates of maize endosperm tissue. The kinase activity requires 10 mM Mg2+ for maximal activity, can utilize either ATP or GTP as phosphate donors and is inhibited by polyamines, heparin and monovalent cations. A substrate specificity of the kinase activity towards specific nuclear proteins is indicated by its phosphorylation of high mobility group (HMG) proteins isolated from endosperm and its lack of accepting histones as protein substrates.
从玉米胚乳组织的细胞核裂解物中分离并富集了一种II型酪蛋白激酶。该激酶活性需要10 mM Mg2+才能达到最大活性，可利用ATP或GTP作为磷酸供体，并受到多胺、肝素和单价阳离子的抑制。从胚乳中分离出的高迁移率族（HMG）蛋白的磷酸化以及其不接受组蛋白作为蛋白质底物，表明了该激酶活性对特定核蛋白的底物特异性。
