JBC, Vol. 251, Issue 20, 6197-6204, Oct, 1976
Purification of a glycoprotein from mouse ascites fluid by immunoaffinity chromatography which is related to the major glycoprotein of murine leukemia viruses. Immunologic and structural comparison with purified viral glycoproteins
S. J. Kennel
Proteins immunologically related to the major glycoprotein from murine
leukemia viruses, gp70, are expressed in the tissue and body fluids of
unmanipulated mice in the absence of virus particle production.
Cross-reactive gp70 was isolated from ascites fluid of NZB and (NZB X
NZW)F1 mice utilizing immunoaffinity chromatography. An enriched antibody
preparation bound to Sepharose was used as an immunosorbent to purify gp70
over 600-fold in one step with a 30% recovery. The gp70s from ascites fluid
were compared with gp70s purified from laboratory virus strains Friend,
Rauscher, Moloney, and Scripps leukemia viruses. Direct antibody binding
studies showed that the viral gp70s were more closely related to each other
than to the gp70s from ascites fluid. Furthermore, the gp70s from ascites
fluid were more reactive with antibody to xenotropic virus than were the
gp70s from the laboratory viruses tested. Tryptic peptide map analysis of
radioiodinated proteins showed that gp70 from Scripps virus is closely
related to gp70 from Moloney virus in primary structure and less closely
related structurally to gp70 from Rauscher virus and gp70 from NZB ascites
fluid.
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