Isolation and chemical characterization of the major envelope glycoprotein of avian myeloblastosis virus.

摘要: The major envelope glycoprotein of avian myeloblastosis virus ( A M V ) has been isolated by disruption the with lithium diiodosalicylate (Lisa& and 2-mercaptoethanol, followed partition 25% phenol. viral RNA remained in aqueous phase. After dialysis addition Triton X100, was separated ion exchange chromatography on DEAJGagarose presence a NaCl gradient detergent. Isoelectric focusing revealed substantial charge heterogeneity, neuraminidase treatment resulting shift toward higher PI values. Determination hydrodynamic volumes sodium dodecyl sulfate or guanidine hydrochloride yielded apparent Mr values 50,000 43,000, respectively, suggesting contribution heterosaccharide to conformation protein different solvents. lipophilic nature manifested binding nonionic detergent X-100, 0.4 mg/mg protein. lack detectable NHz-terminal group indicates possible blocked NH2 terminal group. Cyanogen bromide cleavage 5 methionine residues/mol, as determined from number fragments. From amino acid composition r sidues, an M, 36,600 assigned polypeptide chain. This satisfies requirements accepted model for oncornavirus processing. uneven distribution carbohydrate between products, coupled properties protein, its amphipathic nature.