title: Oligomeric organization of gp120 on infectious human immunodeficiency virus type 1 particles.
abstract: The oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein (gp120) was examined by treating infectious virions with chemical cross-linking agents and subjecting the protein to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and velocity centrifugation. Immunoblots of cross-linked samples revealed three gp120 bands and an approximately threefold shift in gp120 sedimentation. Our finding of cross-linking solely between gp120 suggests that the gp120 subunits are closely associated in the native envelope structure.
authors.affiliation: Cancer Research Institute, School of Medicine, University of California 94143-0450.
authors.forename: C D
authors.initials: CD
authors.lastname: Weiss
authors.forename: J A
authors.initials: JA
authors.lastname: Levy
authors.forename: J M
authors.initials: JM
authors.lastname: White
mesh_terms: D002499:Centrifugation, Density Gradient; D003432:Cross-Linking Reagents; D004591:Electrophoresis, Polyacrylamide Gel; D015699:HIV Envelope Protein gp120 / Q000648:ultrastructure*; D015497:HIV-1 / Q000648:ultrastructure*; D046911:Macromolecular Substances; D011485:Protein Binding
chemical_list: D003432:Cross-Linking Reagents; D015699:HIV Envelope Protein gp120; D046911:Macromolecular Substances