Antibodies against synthetic peptides as a tool for functional analysis of the 
transforming protein pp60src

Tamura, Teruko; Bauer, Heinz; Birr, Christian; Pipkorn, Rüdiger

doi:10.1016/0092-8674(83)90391-4

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Antibodies against synthetic peptides as a tool for functional analysis of the transforming protein pp60src

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Birr, Christian
Max Planck Institute for Medical Research, Max Planck Society;

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Pipkorn, Rüdiger
Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Tamura, T., Bauer, H., Birr, C., & Pipkorn, R. (1983). Antibodies against synthetic peptides as a tool for functional analysis of the transforming protein pp60src. Cell, 34(2), 587-596. doi:10.1016/0092-8674(83)90391-4.

Cite as: https://hdl.handle.net/21.11116/0000-0003-4CB0-1

Abstract

To study the function of pp60src, the transforming protein encoded for by Rous sarcoma virus, we have raised antibodies against synthetic oligopeptides corresponding to the primary structure of pp60src. All eight investigated peptides were immunogenic in rabbits, and four induced pp60src-specific antibodies. We screened tumor-bearing rabbit (TBR) sera for antibodies against the peptides; this revealed that five out of six of the peptides, chosen according to a high hydrophilicity plot, were related to epitopes of native pp60src, in contrast to two peptides of low hydrophilicity, which contained a cleavage site for protease. Antibodies against three of the peptides appeared to react with the kinase-active site of pp60src, as these antibodies were phosphorylated in their heavy chain upon immune precipitation. Antibodies against two of the peptides, in contrast to the others, did not precipitate pp60src when this molecule was complexed with two cellular proteins, pp50 and ppg0. This observation allows speculation about the location of the pp60src site involved in the formation of this complex.