title: Enzymatic protection from autoxidation for crosslinked hemoglobins.
abstract: The autoxidation rates of hemoglobins crosslinked between the alpha subunits (alpha 99XLHb A) and between the beta subunits (beta 82XLHb A) were reduced in the presence of catalase and/or superoxide dismutase. In the presence of catalase the rate for alpha 99XLHb A decreased 2.3 fold and for beta 82XLHb A, 1.9 fold. Superoxide dismutase reduced the rate 1.6 fold for alpha 99XLHb A and 1.8 fold for beta 82XLHb A. In the presence of both catalase and superoxide dismutase the rate of autoxidation decreased by 3.0 fold in alpha 99XLHb A and 4.0 fold in beta 82XLHb A. The presence of catalase and superoxide dismutase or both in the crosslinked hemoglobin samples increases the autoxidation half-life of oxyhemoglobins. This suggests that crosslinked hemoglobins to be used as blood substitutes could be protected from oxidation in storage by these enzymes.
authors.affiliation: Department of Chemistry, Loyola University of Chicago, IL 60626.
authors.forename: T
authors.initials: T
authors.lastname: Yang
authors.forename: K W
authors.initials: KW
authors.lastname: Olsen
mesh_terms: D001241:Aspirin / Q000031:analogs & derivatives / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D001802:Blood Substitutes / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D002374:Catalase; D003432:Cross-Linking Reagents; D004356:Drug Storage; D006207:Half-Life; D006454:Hemoglobins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D008706:Methemoglobin / Q000378:metabolism; D010084:Oxidation-Reduction; D012996:Solutions; D013482:Superoxide Dismutase
chemical_list: D001802:Blood Substitutes; D003432:Cross-Linking Reagents; D006454:Hemoglobins; D012996:Solutions; C053936:hemoglobin XL99alpha; D008706:Methemoglobin; D002374:Catalase; D013482:Superoxide Dismutase; D001241:Aspirin