{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,13]],"date-time":"2026-02-13T05:56:08Z","timestamp":1770962168229,"version":"3.50.1"},"reference-count":31,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2006,7,18]],"date-time":"2006-07-18T00:00:00Z","timestamp":1153180800000},"content-version":"vor","delay-in-days":9256,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Intl Journal of Cancer"],"published-print":{"date-parts":[[1981,3,15]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Mammalian cells transformed in tissue culture by SV40 were shown to contain, in addition to the SV40\u2010coded 94,000 d large T antigen and the 20, 000 d small t antigen, a \u223c 56,000 d cellular protein, which specifically precipitates with sera of animals bearing SV40\u2010induced tumor (s) (tumor or T serum). We investigated the presence of these three proteins at the surface of logarithmically growing SV40\u2010transformed cloned mouse cells, after metabolic labelling with [<jats:sup>35<\/jats:sup>S]\u2010methionine for 3 h. The 56,000 d protein was found to be susceptible to digestion by trypsin under conditions which did not disrupt the cells, while no small t antigen was found to be digested. Both the 56,000 d cellular protein and the SV40 large T antigen were susceptible to lactoperoxi\u2010dase\u2010catalyzed iodination from the outside of intact cells. Trypsin treatment removed both the iodinated 56,000 d protein and the iodinated SV40 large T antigen. These experiments indicated that (a certain amount of) the 56,000 d protein and a relatively small amount of the large T antigen (which is present mainly in the nucleus) are present on the cell surface. The results confirm and extend independent experiments using subcellular frac\u2010tionation techniques (Luborsky and Chandrasekaran, 1980; Soule and Butel, 1979). After heat treatment (at 50\u00b0C for 30 min) of the whole\u2010cell extract the 56,000 d cellular protein was precipitated by the tumor serum in the absence of precipitation of SV40 large T antigen. This result showed that the 56,000 d protein is more (thermostable (in the whole\u2010cell extract) than the SV40 large T antigen, and also indicated that the tumor serum employed had antibodies against the 56,000 d cellular antigen. The heat\u2010treated whole\u2010cell extract of SV40\u2010transformed mouse cells was able to immunize and fully protect mice against a lethal tumorigenic dose of SV40\u2010transformed cells. These results suggest the need for further experiments to characterize the chemical and immunologic properties of the 56,000 d protein.<\/jats:p>","DOI":"10.1002\/ijc.2910270320","type":"journal-article","created":{"date-parts":[[2007,2,19]],"date-time":"2007-02-19T18:15:51Z","timestamp":1171908951000},"page":"397-407","source":"Crossref","is-referenced-by-count":21,"title":["Surface proteins of simian\u2010virus\u201040\u2010transformed cells"],"prefix":"10.1002","volume":"27","author":[{"given":"K.","family":"Chandrasekaran","sequence":"first","affiliation":[]},{"given":"David J.","family":"Winterbourne","sequence":"additional","affiliation":[]},{"given":"Samuel W.","family":"Luborsky","sequence":"additional","affiliation":[]},{"given":"Peter T.","family":"Mora","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2006,7,18]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1128\/jvi.21.2.459-467.1977","article-title":"Expression and thermal stability of simian virus 40 tumor specific transplantation antigen and tumour antigen in wild type and tsA mutant\u2010transformed cells","volume":"21","author":"Anderson J. 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