Spina A, Chiosi E, Illiano G, Berlingieri M T, Fusco A, Grieco M
Cattedra di Chimica Biologica, Dipartimento di Biochimica e Biofisica, Università di Napoli, Italy.
Biochem Biophys Res Commun. 1988 Dec 30;157(3):1093-103. doi: 10.1016/s0006-291x(88)80986-0.
Both cytoplasmic and membrane-bound protein kinase C activities are increased in: Harvey-Sarcoma Virus, infected thyroid epithelial cells. The cytoplasmic kinase C increase is found in the chromatographic fraction eluted at lower salt concentration (100 mM NaCl-S100), while the more acidic protein fraction eluted at higher salt concentration (35 mM NaCl-S350) is virtually absent. Although the cytoplasmic S100 fraction from the control and ras-virus infected cells display a comparable PBt2 binding activity, they are different in the Ca+2-dependence and the TPA down regulation. In addition, the membranes from the control and ras-virus infected cells are different phosphate acceptors in place of the H1 histones.
在感染哈维氏肉瘤病毒的甲状腺上皮细胞中，细胞质和膜结合的蛋白激酶C活性均增加。细胞质激酶C活性的增加出现在低盐浓度（100 mM NaCl - S100）洗脱的色谱级分中，而在高盐浓度（35 mM NaCl - S350）洗脱的酸性更强的蛋白级分中则几乎不存在。尽管来自对照细胞和ras病毒感染细胞的细胞质S100级分显示出相当的PBt2结合活性，但它们在Ca+2依赖性和佛波酯（TPA）下调方面存在差异。此外，对照细胞和ras病毒感染细胞的膜在取代H1组蛋白方面是不同的磷酸受体。
