title: Membrane proteins specified by herpes simplex viruses. IV. Conformation of the virion glycoprotein designated VP7(B2).
abstract: The herpes simplex virus glycoprotein designated VP7(B2) is extracted from virions by nonionic detergent in the form of an oligomer, whereas the other detergent-soluble envelope proteins appear to be extracted as monomers. The subunits of the VP7(B2) oligomer cannot be dissociated by 2-mercaptoethanol and are also resistant to dissociation by a mixture of sodium dodecyl sulfate and 2-mercaptoethanol, except at elevated temperature. The oligomeric form of solubilized VP7(B2) appears to be predominantly dimeric, based on the sedimentation rats in sucrose gradients and the electrophoretic mobilities in sodium dodecyl sulfate-containing acrylamide gels of the undissociated and heat-dissociated forms of VP7(B2).
mesh_terms: D006023:Glycoproteins / Q000032:analysis*; D006358:Hot Temperature; D008623:Mercaptoethanol / Q000494:pharmacology; D011487:Protein Conformation; D018139:Simplexvirus / Q000032:analysis* / Q000187:drug effects; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D012995:Solubility; D013501:Surface-Active Agents / Q000494:pharmacology; D014764:Viral Proteins / Q000032:analysis*
chemical_list: D006023:Glycoproteins; D013501:Surface-Active Agents; D014764:Viral Proteins; D012967:Sodium Dodecyl Sulfate; D008623:Mercaptoethanol