Section 5
Chapter 4,894

Cell surface binding proteins for the major envelope glycoprotein of murine leukemia virus

Twardzik, D.R.; Fowler, A.K.; Weislow, O.S.; Hegamyer, G.A.; Hellman, A.

Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine 162(2): 304-309


ISSN/ISBN: 0037-9727
PMID: 316137
Accession: 004893962

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The 71,000 Mr [relative MW] major envelope glycoprotein (gp71) of Rauscher murine leukemia virus binds to susceptible cells in vitro. [3H]Leucine surface polypeptides bound to 125I-labeled gp71 were stripped from BALB/c thymocytes with nonionic detergent and chemically linked with the cleavable bifunctional reagent methyl 4-mercaptobutyrimidate. Soluble disulfide-linked 125I-labeled gp71 bound thymocyte surface polypeptide oligomers were precipitated with adsorbed gp71 antisera and after reductive cleavage. MW (SDS-PAGE [sodium dodecyl sulfate-polyacrylamide gel electrophoresis]) of approximately 23,000, 32,000, 45,000, 65,000, 90,000 and 170,000 Mr were seen. The cross-linked-dependent immunoprecipitation of 125I-labeled gp71.cntdot.thymocyte surface polypeptide oligomers with antiserum having reactivity to products of the major histocompatibility locus (H-2d and Ia) and for the gag gene products (p30 and p15) was demonstrated. The involvement of these thymocyte surface polypeptides in structuring the functional receptor for ecotropic oncornaviruses is discussed.

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