Purification of the Rous sarcoma virus src kinase by casein-agarose and tyrosine-agarose affinity chromatography.

Publisher Website
Google Scholar
Abstract
A simple and effective purification method for the src kinase, the transforming gene product of Rous sarcoma virus, was developed by using affinity chromatography on casein-agarose and tyrosine-agarose columns. Na-DodSO4/polyacrylamide gel electrophoresis and Ag staining analysis showed that the purified kinase preparation was composed of a predominant polypeptide of 60,000-Da [Daltons]. In most of the preparations, however, 3 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 phosphorylated on tyrosine by the purified src kinase.