PHORBOL DIESTER RECEPTOR CO-PURIFIES WITH PROTEIN KINASE-C
PHORBOL DIESTER RECEPTOR CO-PURIFIES WITH PROTEIN KINASE-C
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DOI：
10.1073/pnas.80.1.36
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发表时间：
1983-01-01
期刊：
影响因子：
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通讯作者：
VANDENBARK, GR
中科院分区：
文献类型：
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作者：
NIEDEL, JE;KUHN, LJ;VANDENBARK, GR
在没有洗涤剂的情况下，二价离子螯合可溶解存在于大鼠脑颗粒部分中的佛波二酯[肿瘤启动子]受体。可溶性受体通过（NH4）2SO4沉淀、deae -纤维素和凝胶过滤层析进行部分纯化。纯化后的受体需要外源磷脂才能发挥活性，对[3H]磷酸12,13-二丁酸酯的Kd值为7 nM。生物活性磷类似物抑制结合，而无活性类似物则没有。依赖于Ca2+的磷脂敏感蛋白激酶C与磷受体共化。纯化后的蛋白激酶C在磷脂存在的情况下被12-肉豆蔻酸13-乙酸佛波直接激活。
The phorbol diester [tumor promoter] receptor present in the particulate fraction of rat brain was solubilized by divalent ion chelation in the absence of detergents. The soluble receptor was partially purified by (NH4)2SO4 precipitation, DEAE-cellulose and gel filtration chromatography. The purified receptor required exogenous phospholipid for activity and displayed a Kd of 7 nM for [3H]phorbol 12,13-dibutyrate. Biologically active phorbol analogs inhibited binding, whereas inactive analogs did not. The Ca2+-dependent, phospholipid-sensitive protein kinase C copurified with the phorbol receptor. Purified protein kinase C was activated directly by phorbol 12-myristate 13-acetate in the presence of phospholipid.