title: [Assessment of the composition and structure of covalent complexes of superoxide dismutase with aldehyde dextran by analytical ultracentrifugation].
abstract: Superoxide dismutase was covalently coupled wih aldehyde dextran, a polymeric carrier of molecular mass of 70 kDa. Modification produced an increase in the enzyme thermostability. Modified preparations retained a high specific activity. The composition of the thus obtained conjugates was analyzed by the ultracentrifugation and diffusion methods. The protein induced the destruction of aldehyde dextran, the enzyme being modified by its fragments. The presence of aldehyde dextran excess in the incubation medium promoted superoxide dismutase dissociation into individual subunits. At the enzyme/carrier ratio of 1:02 modification occurred as covalent coupling of the biocatalyst subunits and its one-point modification.
authors.forename: A V
authors.initials: AV
authors.lastname: Maksimenko
authors.forename: E L
authors.initials: EL
authors.lastname: Grigor'eva
authors.forename: A D
authors.initials: AD
authors.lastname: Morozkin
authors.forename: E G
authors.initials: EG
authors.lastname: Tishchenko
authors.forename: E B
authors.initials: EB
authors.lastname: Minkovskiĭ
authors.forename: V P
authors.initials: VP
authors.lastname: Torchilin
mesh_terms: D003911:Dextrans / Q000737:chemistry*; D004058:Diffusion; D013482:Superoxide Dismutase / Q000737:chemistry*; D014461:Ultracentrifugation
chemical_list: D003911:Dextrans; D013482:Superoxide Dismutase
vernacular_title: Otsenka sostava i stroeniia kovalentnykh kompleksov superoksiddismutazy s al'degiddekstranom metodom analiticheskogo ul'tratsentrifugirovaniia.