Binding of proteins, including pp60src, to activated CH-Sepharose 4B

• Published in: Molecular biology reports Vol. 12; no. 2; pp. 127 - 131
• Main Authors: PAVLOFF, N, BIQUARD, J.-M, MARILLER, M, RABOTTI, G. C, FOSSAR, N, GAY, F, SEMMEL, M
• Format: Journal Article
• Language: English
• Published: Dordrecht Kluwer 01-01-1987
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Chick Embryo; Fundamental and applied biological sciences. Psychology; General aspects, investigation methods; Oncogene Protein pp60(v-src); Protein Binding; Proteins; Rabbits; Retroviridae Proteins - metabolism; Sepharose - analogs & derivatives; Sepharose - metabolism; Staphylococcal Protein A - metabolism; Proteins; Molecular interaction
• ISSN: 0301-4851; 1573-4978
• DOI: 10.1007/BF00368881

Activated CH-Sepharose 4B and protein A Sepharose CL-4B can bind, selectively and non-specifically, polypeptides from chick embryo cells. The major polypeptides bound have apparent molecular masses of 57-60 kDa and 47-49 kDa and cannot be eluted by extensive washing with buffers containing detergents. One of the 57-60 kDa polypeptides was identified by immunoblotting as the transforming protein of Rous Sarcoma Virus (RSV), pp60src. This polypeptide could be removed from the solid phase immunoabsorbent with 60% dimethylsulfoxide, but not with 2% SDS, 5% beta-mercaptoethanol, 1 M NaCl or 0.1% Tween 20.