Proteins of Rous-associated virus type 61: polypeptide stoichiometry and evidence that glycoprotein gp35 is not a cleavage product of gp85.
The two glycoproteins, gp85 and gp35, of Rous-associated virus type 61 (RAV-61), were isolated from radiolabeled virions by gel electrophoresis and digested with trypsin. The chromatographic profile of the gp35 digest revealed no peaks in common with that of gp85; therefore, the smaller glycoprotein is not a cleavage product of gp85. The stoichiometry of radiolabeled RAV-61 proteins was studied by quantitative gel filtration and gel electrophoresis. Among the 11 polypeptides identified were 4 minor ones, including the beta(p91) and alpha(p64) chains of reverse transcriptase and two unidentified chains, p76 and p35; the latter two were unmasked by removing the virions' surface glycoproteins with a protease, bromelain. Virions contained some 15 to 30 molecules of reverse transcriptase.
D000818:Animals; D001354:Avian Leukosis Virus / Q000032:analysis* / Q000201:enzymology; D002642:Chick Embryo; D046508:Culture Techniques; D006023:Glycoproteins / Q000032:analysis*; D010455:Peptides / Q000032:analysis; D012194:RNA-Directed DNA Polymerase / Q000032:analysis; D014764:Viral Proteins / Q000032:analysis*
D006023:Glycoproteins; D010455:Peptides; D014764:Viral Proteins; D012194:RNA-Directed DNA Polymerase