A study on the thermal stability of bovine Cu, Zn superoxide dismutase : the effects of ionic strength and solution composition

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dc.contributor.advisor Johnson, Eric R. en_US
dc.contributor.author Williams, Douglas B. en_US
dc.date.accessioned 2011-06-03T19:32:35Z
dc.date.available 2011-06-03T19:32:35Z
dc.date.created 1979 en_US
dc.date.issued 1979
dc.identifier LD2489.Z78 1979 .W54 en_US
dc.identifier.uri http://cardinalscholar.bsu.edu/handle/handle/182052
dc.description.abstract The following thesis examines the effects of ionic strength and solution composition on the thermal stability and. activity of bovine erythrocyte superoxide dismutase (BESOD). An indirect assay procedure was employed. The oxidation of xanthine, catalyzed by xanthine oxidase, served as a generator of superoxide radicals (02) and ferricytochrome c functioned as a scavenger of these radicals. The assays were monitored and recorded spectrophotometrically. Percent superoxide dismutase activity remaining after a 30 minute heat treatment and 241 hours after the heat treatment were determined. As the concentration and computed ionic strength values of the ionic solutions increased, the percent BESOD activity remaining after 30 minutes at 80 C decreased. Recovery of BESOD activity after 24 hours was minimal in all ionic solutions. BESOD denaturation was apparently similar in the chloride and sulfate solutions, but much greater in the phosphate solutions. Mathematical interpretation confirmed the similar relationships between chloride and sulfate solutions, and the much greater effects of phosphate solutions on thermal denaturation of SOD. At concentrations of 10-1 M or less, thermal denaturation of SOD was greatest, implying the appearance of a denaturation threshold. A specific phosphate effect may be apparent and was described by two models: 1- complexation of Cut + ions with phosphate anions, and 2- conformational alteration due to charge repulsion between molecular strands of the SOD molecule. Both of these models could be possible explanations as to the much greater thermal denaturation observed in the phosphate solutions.
dc.format.extent iii, 46 leaves : ill. ; 28 cm. en_US
dc.source Virtual Press en_US
dc.subject.lcsh Dismutase. en_US
dc.subject.lcsh Enzyme inhibitors. en_US
dc.subject.lcsh Biochemistry. en_US
dc.title A study on the thermal stability of bovine Cu, Zn superoxide dismutase : the effects of ionic strength and solution composition en_US
dc.title.alternative Bovine Cu, Zn superoxide dismutase. en_US
dc.description.degree Thesis (M.S.)
dc.identifier.cardcat-url http://liblink.bsu.edu/catkey/262096 en_US


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  • Master's Theses [5510]
    Master's theses submitted to the Graduate School by Ball State University master's degree candidates in partial fulfillment of degree requirements.

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