title: [Fibrillar actin promotes assembly of dissociated 20S-proteasome complex].
abstract: 20S-proteasome was purified from rat liver cells by ultracentrifugation, gel-chromatography and ultrafiltration. The ability of 20S-proteasome to interact with fibrillar actin (F-actin) was examined by rapid cosidementation of these dissociated particles with F-actin in isokinetic sucrose gradient. Proteasomes, which were dissociated with Zn2+ ions, can be assembled on the fibrillar actin once again (with the exception of protein 27 kDa) at deleting ions Zn2+ from the solution with the help of EDTA.
authors.affiliation: Institute of Cytology RAS, St. Petersburg.
authors.forename: V E
authors.initials: VE
authors.lastname: Galkin
authors.forename: V N
authors.initials: VN
authors.lastname: Babakov
authors.forename: L V
authors.initials: LV
authors.lastname: Turoverova
authors.forename: I M
authors.initials: IM
authors.lastname: Konstantinova
authors.forename: G P
authors.initials: GP
authors.lastname: Pinaev
mesh_terms: D000199:Actins / Q000378:metabolism*; D000818:Animals; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D008099:Liver / Q000378:metabolism; D008297:Male; D009097:Multienzyme Complexes / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D011485:Protein Binding; D051381:Rats
chemical_list: D000199:Actins; D009097:Multienzyme Complexes; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex