Guasch M D, Plana M, Pena J M, Itarte E
Biochem J. 1986 Mar 15;234(3):523-6. doi: 10.1042/bj2340523.
Casein kinase 2 from rat liver cytosol phosphorylated human fibrinogen in a reaction that was not stimulated by Ca2+ or cyclic AMP, but was markedly inhibited by heparin, and proceeded at a similar rate when either ATP or GTP was used as phosphate donor. Analysis of casein kinase 2 by glycerol-density-gradient centrifugation showed that the activities towards fibrinogen, casein, phosvitin, high-mobility-group protein 14 and glycogen synthase coincided. Maximal incorporation into fibrinogen by casein kinase 2 averaged 1 mol of phosphate/mol of protein substrate, most of it in the alpha-chain, although some phosphorylation of the beta-chain was also detected. Analysis of phosphorylated alpha-chain revealed that most of the phosphate was incorporated on serine. Phosphorylation of human fibrinogen was also performed by casein kinase 2 from human polymorphonuclear leucocytes, lymphocytes and platelets.
来自大鼠肝细胞溶胶的酪蛋白激酶2在一个既不受Ca2+或环磷酸腺苷刺激，又明显受肝素抑制的反应中使人类纤维蛋白原磷酸化。当使用ATP或GTP作为磷酸供体时，该反应以相似的速率进行。通过甘油密度梯度离心法对酪蛋白激酶2进行分析表明，其对纤维蛋白原、酪蛋白、卵黄高磷蛋白、高迁移率族蛋白14和糖原合酶的活性是一致的。酪蛋白激酶2使纤维蛋白原的最大磷酸掺入量平均为每摩尔蛋白质底物1摩尔磷酸盐，其中大部分在α链上，不过也检测到了β链的一些磷酸化。对磷酸化α链的分析表明，大部分磷酸盐掺入到了丝氨酸上。来自人类多形核白细胞、淋巴细胞和血小板的酪蛋白激酶2也能使人类纤维蛋白原磷酸化。
