Purification of murine and feline type-C virus envelope polypeptides as micellar protein complexes.
A technique originally described for the isolation of Friend leukaemia virus envelope polypeptides [1] yields equivalent structures from Moloney leukaemia. AKR and BALB/c xenotropic virus as well as feline leukaemia virus. The envelope polypeptides are obtained as micellar protein complexes, named rosettes. Rosettes of the five mammalian type-C viruses examined are indistinguishable by electron microscopy. Separation of these aggregates in polyacrylamide gel electrophoresis under nonreducing conditions reveals a glycoprotein of about 85000 d as their major component. Tryptic peptide analyses identify the viral origin of these polypeptides and emphasize strain specific differences in their primary structure.
D000818:Animals; D002415:Cats; D051379:Mice; D008823:Micelles; D008854:Microscopy, Electron; D008970:Molecular Weight; D010446:Peptide Fragments; D010455:Peptides / Q000302:isolation & purification*; D012190:Retroviridae / Q000032:analysis*; D012397:Rosette Formation; D013045:Species Specificity; D014357:Trypsin; D014764:Viral Proteins / Q000302:isolation & purification*
D008823:Micelles; D010446:Peptide Fragments; D010455:Peptides; D014764:Viral Proteins; D014357:Trypsin