title: Evidence indicating that the human proteasome is a complex dimer.
abstract: Using monoclonal antibodies and electron microscopy, the relative positions of two subunit species (32 kDa, pI 6.8; 28.4 kDa, pI 7.9) have been determined on the proteasome (multicatalytic proteinase). From the epitope occupancy, it appears that both subunits occur twice in a proteasome: once in each of the two terminal disks that close off the barrel-like particle. The result favors a model of a complex dimer, and is discussed in the light of the architectural concept that has emerged from our recent immunoelectron microscopic studies of the less complex archaebacterial proteasome.
authors.affiliation: Diabetes Forschungsinstitut an der Universität Düsseldorf, Germany.
authors.forename: F
authors.initials: F
authors.lastname: Kopp
authors.forename: B
authors.initials: B
authors.lastname: Dahlmann
authors.forename: K B
authors.initials: KB
authors.lastname: Hendil
mesh_terms: D000911:Antibodies, Monoclonal; D001665:Binding Sites; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000648:ultrastructure; D000939:Epitopes / Q000032:analysis; D006801:Humans; D008854:Microscopy, Electron; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000648:ultrastructure; D046988:Proteasome Endopeptidase Complex
chemical_list: D000911:Antibodies, Monoclonal; D000939:Epitopes; D009097:Multienzyme Complexes; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex