title: Superoxide dismutase: improving its pharmacological properties by conjugation with human serum albumin.
abstract: Superoxide Dismutase has been reported to offer important pharmacological advantages in modifying oxygen toxicity as a result of its ability to scavenge oxygen free radicals. This has proven most exciting in reducing damage associated with post-reperfusion damage following myocardial ischemia. Unfortunately Superoxide Dismutase has a circulation life time of only a few minutes making the exact time of its administration crucial and somewhat impractical. We report here on the production of SOD-Albumin conjugates which have important advantages over free SOD in terms of stability, extended circulation time and reduced immunogenicity.
authors.affiliation: Department of Physiology, Faculty of Medicine, University of Alberta, Edmonton, Canada.
authors.forename: G D
authors.initials: GD
authors.lastname: Mao
authors.forename: M J
authors.initials: MJ
authors.lastname: Poznansky
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D004356:Drug Storage; D004795:Enzyme Stability; D006861:Hydrogen Peroxide / Q000494:pharmacology; D008657:Metabolic Clearance Rate; D051379:Mice; D008807:Mice, Inbred BALB C; D051381:Rats; D011919:Rats, Inbred Strains; D012709:Serum Albumin / Q000276:immunology / Q000493:pharmacokinetics; D013482:Superoxide Dismutase / Q000276:immunology / Q000493:pharmacokinetics
chemical_list: D012709:Serum Albumin; D006861:Hydrogen Peroxide; D013482:Superoxide Dismutase