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Localization of subunits in proteasomes from Thermoplasma acidophilum by immunoelectron microscopy
Author(s) -
Grziwa Anja,
Baumeister Wolfgang,
Dahlmann Burkhardt,
Kopp Friedrich
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81256-8
Subject(s) - thermoplasma acidophilum , immunoelectron microscopy , protein subunit , proteasome , biology , biochemistry , microbiology and biotechnology , chemistry , biophysics , antibody , enzyme , genetics , gene
The subunit topography of the Thermoplasma acidophilum proteasome was determined by iminunoelectron microscopy using monospecific antibodies directed against the two constituent subunits (α,β). Anti‐α‐subunit IgG was found to bind to the outer disks of the cylinder‐ or barrel‐shaped molecule, while the binding sites of the anti‐β‐subunit IgG were mapped on the two inner rings. Probably the homologues of the two subunits in the compositionally more complex but isomorphous eukaryotic proteasomes occupy equivalent positions.

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