Antibodies of predetermined specificity detect two retroviral oncogene products and inhibit their kinase activities
Article
Sen, S, Houghten, RA, Sherr, CJ et al. (1983). Antibodies of predetermined specificity detect two retroviral oncogene products and inhibit their kinase activities
. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 80(5 I), 1246-1250. 10.1073/pnas.80.5.1246
Sen, S, Houghten, RA, Sherr, CJ et al. (1983). Antibodies of predetermined specificity detect two retroviral oncogene products and inhibit their kinase activities
. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 80(5 I), 1246-1250. 10.1073/pnas.80.5.1246
Oligopeptides predicted from the nucleotide sequence of the oncogene v-fes of feline sarcoma virus (FeSV) were synthesized chemically and used to generate specific antibodies. Antisera against a 12-amino-acid-long oligopeptide (12-mer) located 42 residues from the carboxyl terminus of the v-fes coding sequence efficiently recognized the transforming proteins encoded by Snyder-Theilen (ST) and Gardner-Arnstein (GA) strains of FeSV. This 12-mer also contains 10 amino acid residues homologous in order and position to those predicted from the nucleotide sequence of the oncogene v-fps of avian Fujinami sarcoma virus (FSV). The anti-12-mer immunoprecipitated the FSV-specific transforming protein molecules from FSV-transformed cells. Binding of these antipeptide antibody molecules to the v-fes and the v-fps gene products inhibited their associated tyrosine-specific protein kinase (EC 2.7.1.37) activities. The ability to generate such site-specific antisera to the products of related oncogenes will be valuable in the molecular characterization of retroviral transforming proteins and their normal cellular homologs.
