Human p85 glycoprotein bears three distinct epitopes defined by several monoclonal antibodies

作者: Michelle Letarte , None

DOI: 10.1016/0161-5890(86)90101-X

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摘要: A glycoprotein of apparent mol. wt 85,000 isolated from human cells B lineage by affinity to 50B4-IgG immunoadsorbent was shown previously express two spatially distinct epitopes identified with monoclonal antibodies 50B4 and 50E6 [Letarte et al. (1985) Molec. Immun. 22, 113-124]. It is now demonstrated that the p85 homologous F10-44-2 antigen, defined initially as a T-lymphocyte-granulocyte-brain antigen [Dalchau (1980) Eur. J. 10, 745-749], A1G3 medullary thymocyte [Haynes (1983) 131, 1195-1200] A3D8 on erythrocytes [Telen clin. Invest. 71, 1878-1886]. The purified either lymphoblastoid cell line or leukemic line, at concn ranging 0.25 2.0 micrograms protein/ml, could block binding F-10-62-1 (a related antibody) cells. All these immunoprecipitated, antigenic preparation, single glycosylated polypeptide chain 85,000. Competitive studies indicated define least three epitopes. blocked reactivity 50E6-IgG thus bind an epitope identical epitope. Antibody F10-62-1 competed for recognizes 50B4-like antibody 30% but did not inhibit 50B4-IgG: it reacting third close

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