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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Bibliographic Details
Published inMolecular biology reports Vol. 12; no. 2; p. 127
Main Authors Pavloff, N, Biquard, J M, Mariller, M, Rabotti, G C, Fossar, N, Gay, F, Semmel, M
Format Journal Article
LanguageEnglish
Published Netherlands 01.01.1987
Subjects
Animals
Chick Embryo
Oncogene Protein pp60(v-src)
Protein Binding
Rabbits
Retroviridae Proteins - metabolism
Sepharose - analogs & derivatives
Sepharose - metabolism
Staphylococcal Protein A - metabolism
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Summary: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
DOI:10.1007/BF00368881