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SDS\u2010PAGE analysis of anti\u2010T immunoprecipitates of SV40\u2010transformed and \u2010infected cells labelled with <jats:sup>125<\/jats:sup>I\/LPO revealed the presence of iodinated T\u2010ag. Several types of control experiments were employed to guarantee the surface specificity of the <jats:sup>125<\/jats:sup>I\/LPO labelling technique. When SV40\u2010transformed mouse cells were surface labelled with lactoperoxidase and glucose oxidase immobilized on insoluble beads, a preparation less readily internalized than soluble enzymes, T\u2010ag was iodinated. Selective immunoprecipitation of surface antigens demonstrated that lactoperoxidase did not iodinate internally localized T\u2010ag. A reconstruction experiment in which an extract of SV40\u2010infected cells was added to uninfected cells prior to surface labelling suggested that T\u2010ag released from lysed cells did not adhere significantly to monolayer surfaces and become iodinated. Finally, systematic omission of reactants from the iodination reaction revealed that exogenous addition of lactoperoxidase and H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub> was necessary to generate an iodinated T\u2010ag, indicating that endogenous host cell reactants do not contribute significantly to the iodination of T\u2010ag. <jats:sup>125<\/jats:sup>I\u2010labelled T\u2010ag was detectable on the surface of SV40 tsA\u2010infected cells at the nonpermissive temperature 24 h post infection, indicating that the tsA lesion does not prevent the interaction of T\u2010ag with the cell surface. When <jats:sup>125<\/jats:sup>I\/LPO\u2010labelled transformed or infected cells were chased for 2.5 h after labelling, iodinated T\u2010ag was no longer associated with the cell monolayer but was immunoprecipitable from culture supernatants. Cultures from which labelled T\u2010ag had been shed could then be relabelled with <jats:sup>125<\/jats:sup>I\/LPO and surface\u2010associated T\u2010ag was again detectable. These data suggest that surface\u2010associated T\u2010ag is continuously shed from the cell surface and is rapidly replaced in the membrane by intracellular T\u2010ag.<\/jats:p>","DOI":"10.1002\/ijc.2910290318","type":"journal-article","created":{"date-parts":[[2007,2,19]],"date-time":"2007-02-19T18:41:29Z","timestamp":1171910489000},"page":"337-344","source":"Crossref","is-referenced-by-count":27,"title":["Detection of simian virus 40 surface\u2010associated large tumor antigen by enzyme\u2010catalyzed radioiodination"],"prefix":"10.1002","volume":"29","author":[{"given":"Howard R.","family":"Soule","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Robert E.","family":"Lanford","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Janet S.","family":"Butel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2006,7,17]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1128\/jvi.35.1.157-164.1980","article-title":"Control of simian virus 40 gene expression at the levels of RNA synthesis and processing: thermally induced changes in the ratio of the simian virus 40 early mRNA's and proteins","volume":"35","author":"Alwine J. 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