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Antibodies were raised against a synthetic peptide corresponding to 14 amino acid residues at the COOH-terminus of a protein deduced from the human c-erbB-2 nucleotide sequence. These antibodies immunoprecipitated a 185-kilodalton glycoprotein from MKN-7 adenocarcinoma cells. Incubation of the immunoprecipitates with (gamma-32P)ATP resulted in the phosphorylation of this protein on tyrosine residues. These results indicate that the human c-erbB-2 gene product is the 185-kilodalton glycoprotein that is associated with tyrosine kinase activity. Although the c-erbB-2 protein was predicted to encode a protein very similar to epidermal growth factor (EGF) receptor, EGF did not stimulate this kinase activity either in vivo or in vitro.
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Tetsu Akiyama
Quantitative BioSciences
Chie Sudo
National Institute of Health Sciences
Hiroshi Ogawara
Kanazawa University
Science
Tokyo Medical University
Tokyo Institute of Psychiatry
Meiji (Japan)
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Akiyama et al. (Fri,) studied this question.
synapsesocial.com/papers/6a0886929a6c4ba6e610b041 — DOI: https://doi.org/10.1126/science.3012781