Christiansen N O, Larsen C S, Juhl H, Esmann V
Biochim Biophys Acta. 1986 Oct 29;884(1):54-9. doi: 10.1016/0304-4165(86)90226-6.
Membrane-associated protein kinases in human polymorphonuclear leukocytes were studied. In unstimulated polymorphonuclear leukocytes the protein kinase C was predominantly present in the cytosol but in phorbol 12-myristate 13-acetate- (PMA-) activated cells a time and dose-dependent translocation of the kinase to the particulate fraction occurred. Two new protein kinase activities also appeared in the particulate fraction upon PMA activation. The one had a Mr of 40,000 and its activity was independent of phospholipids. The other (Mr 90,000) as partially activated by phospholipids, but separated from protein kinase C on DEAE-cellulose chromatography.
对人多形核白细胞中的膜相关蛋白激酶进行了研究。在未受刺激的多形核白细胞中，蛋白激酶C主要存在于胞质溶胶中，但在佛波醇12 -肉豆蔻酸酯13 -乙酸酯（PMA）激活的细胞中，该激酶会发生时间和剂量依赖性的向颗粒部分的转位。在PMA激活后，颗粒部分还出现了两种新的蛋白激酶活性。一种的相对分子质量为40,000，其活性不依赖于磷脂。另一种（相对分子质量90,000）部分被磷脂激活，但在DEAE -纤维素柱层析上与蛋白激酶C分离。
