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dc.contributor.advisorCarter, Dean E.en_US
dc.contributor.authorGustafson, Richard Allan, 1958-
dc.creatorGustafson, Richard Allan, 1958-en_US
dc.date.accessioned2013-04-03T13:15:56Z
dc.date.available2013-04-03T13:15:56Z
dc.date.issued1992en_US
dc.identifier.urihttp://hdl.handle.net/10150/278192
dc.description.abstractThe identification of chlorinated organic compounds in drinking supplies has resulted in an interest in the metabolism and toxicity of chlorinated aldehydes. Another possible factor in the metabolism of chloroaldehydes is the endogenaous tripeptide glutathione. The formation of glutathioneconjugates with chloroaldehydes may increase or decrease their rate of reaction with the aldehyde dehydrogenase enzyme. This study found that the rat liver aldehyde dehydrogenase isozymes lost activity with time regardless of storage conditions. In vitro assays of enzyme activity confirmed substrate specificity for the chloroaldehydes and the isozymes. The reaction rate of glutathione depletion by monochloroacetaldehyde was the highest of the aldehydes. The addition of glutathione to the activity assays resulted in a decrease in Vmax but few significant changes in the Km values. Glutathione concentration was depleted by aldehydes in solution. Glutathione effected the metabolism of aldehydes by aldehyde dehydrogenase isozymes.
dc.language.isoen_USen_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.subjectHealth Sciences, Toxicology.en_US
dc.titleEffect of reduced glutathione on the metabolism of chloroaldehydes by rat liver aldehyde dehydrogenaseen_US
dc.typetexten_US
dc.typeThesis-Reproduction (electronic)en_US
thesis.degree.grantorUniversity of Arizonaen_US
thesis.degree.levelmastersen_US
dc.identifier.proquest1349481en_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.nameM.S.en_US
dc.identifier.bibrecord.b27702546en_US
refterms.dateFOA2018-06-16T16:55:54Z
html.description.abstractThe identification of chlorinated organic compounds in drinking supplies has resulted in an interest in the metabolism and toxicity of chlorinated aldehydes. Another possible factor in the metabolism of chloroaldehydes is the endogenaous tripeptide glutathione. The formation of glutathioneconjugates with chloroaldehydes may increase or decrease their rate of reaction with the aldehyde dehydrogenase enzyme. This study found that the rat liver aldehyde dehydrogenase isozymes lost activity with time regardless of storage conditions. In vitro assays of enzyme activity confirmed substrate specificity for the chloroaldehydes and the isozymes. The reaction rate of glutathione depletion by monochloroacetaldehyde was the highest of the aldehydes. The addition of glutathione to the activity assays resulted in a decrease in Vmax but few significant changes in the Km values. Glutathione concentration was depleted by aldehydes in solution. Glutathione effected the metabolism of aldehydes by aldehyde dehydrogenase isozymes.


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