The major polypeptides of the murine-mammary-tumor virus isolated by plant-lectin affinity chromatography.
Solubilized polypeptides of the murine mammary tumor virus (MuMT virus) were chromatographed on a column of immobilised concanavalin A. The unbound viral material was rechromatographed on phosphocellulose, resulting in the isolation of the major proteins with a molecular weight of 28000 (p28) and 12000 (p12) respectively. The adsorbed glycopolypeptides after elution with methyl alpha-D-mannopyranoside were subjected to gel filtration. The major glycoprotein with a molecular weight of 52000 (gp52) was obtained in an almost pure form. However, a considerable part of gp52 elutes together with a glycoprotein with a molecular weight of 36000 (gp36), suggesting that in addition to the free form of gp52 a complex exists of gp52 plus gp36.
D002846:Chromatography, Affinity / Q000379:methods; D003208:Concanavalin A; D006023:Glycoproteins / Q000302:isolation & purification; D005779:Immunodiffusion; D008324:Mammary Tumor Virus, Mouse / Q000032:analysis* / Q000302:isolation & purification; D008970:Molecular Weight; D010455:Peptides / Q000302:isolation & purification*; D012995:Solubility; D014764:Viral Proteins / Q000302:isolation & purification
D006023:Glycoproteins; D010455:Peptides; D014764:Viral Proteins; D003208:Concanavalin A