Purification of the Rous sarcoma virus src kinase by casein-agarose and tyrosine-agarose affinity chromatography.
Purification of the Rous sarcoma virus src kinase by casein-agarose and tyrosine-agarose affinity chromatography.
复制标题
通过酪蛋白-琼脂糖和酪氨酸-琼脂糖亲和层析纯化劳斯肉瘤病毒 src 激酶。
DOI：
10.1073/pnas.82.2.321
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发表时间：
1985
影响因子：
11.1
通讯作者：
F. Lipmann
中科院分区：
文献类型：
--
作者：
Y. Fukami;F. Lipmann
利用酪蛋白-琼脂糖和酪氨酸-琼脂糖亲和层析柱，建立了一种简单有效的纯化Rous肉瘤病毒转化基因产物src激酶的方法。NaDodSO 4/聚丙烯酰胺凝胶电泳和银染分析表明，纯化的激酶制剂由60，000 Da的主要多肽组成，但在大多数制剂中也检测到三种次要蛋白（54，000、52，000和15，000 Da），并对其进行了部分表征。钙调素作为外源性底物之一，可被纯化的src激酶磷酸化。
A simple and effective purification method for the src kinase, the transforming gene product of Rous sarcoma virus, has been developed by using affinity chromatography on casein-agarose and tyrosine-agarose columns. NaDodSO4/polyacrylamide gel electrophoresis and silver staining analysis showed that the purified kinase preparation was composed of a predominant polypeptide of 60,000-Da. In most of the preparations, however, three minor proteins (54,000, 52,000, and 15,000 Da) were also detected, and they were partially characterized. As one of the exogenous substrates, calmodulin was found to be phosphorylated on tyrosine by the purified src kinase.