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

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 detergent...

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Veröffentlicht in:Molecular biology reports 1987-01, Vol.12 (2), p.127-131
Hauptverfasser: PAVLOFF, N, BIQUARD, J.-M, MARILLER, M, RABOTTI, G. C, FOSSAR, N, GAY, F, SEMMEL, M
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Sprache:eng
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Zusammenfassung: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.
ISSN:0301-4851
1573-4978
DOI:10.1007/BF00368881