THE EFFECT OF QUERCETIN ON THE PHOSPHORYLATION ACTIVITY OF THE ROUS-SARCOMA VIRUS TRANSFORMING GENE-PRODUCT INVITRO AND INVIVO
THE EFFECT OF QUERCETIN ON THE PHOSPHORYLATION ACTIVITY OF THE ROUS-SARCOMA VIRUS TRANSFORMING GENE-PRODUCT INVITRO AND INVIVO
复制标题
DOI：
10.1111/j.1432-1033.1983.tb07692.x
复制
发表时间：
1983-01-01
期刊：
影响因子：
--
通讯作者：
ERIKSON, RL
中科院分区：
文献类型：
--
作者：
GRAZIANI, Y;ERIKSON, E;ERIKSON, RL
生物类黄酮槲皮素在体外和体内均抑制劳斯肉瘤病毒src基因产物pp60src的磷酸转移酶活性。在体外条件下，抑制作用的Ki值在6 - 11μM范围内。槲皮素对作为pp60src底物的核苷酸ATP和GTP的抑制作用是竞争性的，而对作为该激酶活性蛋白质底物的α - 酪蛋白的抑制作用是非竞争性的。对依赖cAMP的蛋白激酶催化亚基的磷酸转移酶活性的体外研究表明，这种类黄酮不抑制该酶生理底物的磷酸化。在培养的[鸡胚成纤维细胞]中，对pp60src的酪氨酸磷酸化以及分子量为34000的蛋白质（pp60src的一种生理底物）磷酸化的半数最大抑制浓度在0.06 - 0.08 mM范围内。
The phosphotransferase activity of the Rous sarcoma virus src gene product, pp60src, was inhibited both in vitro and in vivo by the bioflavonoid quercetin. The Ki for the inhibitory effect was in the range of 6-11 .mu.M under conditions in vitro. The inhibitory effect of quercetin was competitive towards the nucleotides ATP and GTP as substrates for pp60scc and was non-competitive towards .alpha.-casein as the protein substrate of this kinase activity. Studies in vitro of the phosphotransferase activity of the catalytic subunit of the cAMP-dependent protein kinase showed that this flavonoid did not inhibit the phosphorylation of physiological substrates of this enzyme. In cultured [chicken embryo fibroblast] cells the half-maximal inhibition of tyrosine phosphorylation of pp60src as well as the phosphorylation of the MW = 34,000 protein, a physiological substrate of pp60src, was in the range 0.06-0.08 mM.