Substrate specificity of rat liver aldehyde dehydrogenase with chloroacetaldehydes

Persistent Link:
http://hdl.handle.net/10150/277906
Title:
Substrate specificity of rat liver aldehyde dehydrogenase with chloroacetaldehydes
Author:
Sharpe, Amy-Joan Lorna, 1965-
Issue Date:
1991
Publisher:
The University of Arizona.
Rights:
Copyright © 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.
Abstract:
Chlorinated acetaldehydes have recently been the focus of research due to their role as reactive intermediates and their possible occurrence in chlorinated drinking water. The metabolism of these compounds, however, has not been extensively studied. In this study, the in vitro substrate specificity of cytosolic and mitochondrial rat liver aldehyde dehydrogenase toward these compounds was investigated. Both crude and semi-purified preparations of the enzymes were used. Monochloroacetaldehyde was found to be extensively metabolized by this enzyme system. It was metabolized to a greater extent than the standard compound propionaldehyde. Dichloroacetaldehyde was also found to be metabolized by this enzyme, but to a lesser extent than its monochloro-analogue. There was some evidence to suggest, however, that alcohol dehydrogenase and chloral hydrate dehydrogenase may play a significant role in the metabolism of this compound. Chloral hydrate was not metabolized by this enzyme to an appreciable extent.
Type:
text; Thesis-Reproduction (electronic)
Keywords:
Health Sciences, Toxicology.; Biology, Animal Physiology.
Degree Name:
M.S.
Degree Level:
masters
Degree Program:
Graduate College
Degree Grantor:
University of Arizona
Advisor:
Carter, Dean E.

Full metadata record

DC FieldValue Language
dc.language.isoen_USen_US
dc.titleSubstrate specificity of rat liver aldehyde dehydrogenase with chloroacetaldehydesen_US
dc.creatorSharpe, Amy-Joan Lorna, 1965-en_US
dc.contributor.authorSharpe, Amy-Joan Lorna, 1965-en_US
dc.date.issued1991en_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.description.abstractChlorinated acetaldehydes have recently been the focus of research due to their role as reactive intermediates and their possible occurrence in chlorinated drinking water. The metabolism of these compounds, however, has not been extensively studied. In this study, the in vitro substrate specificity of cytosolic and mitochondrial rat liver aldehyde dehydrogenase toward these compounds was investigated. Both crude and semi-purified preparations of the enzymes were used. Monochloroacetaldehyde was found to be extensively metabolized by this enzyme system. It was metabolized to a greater extent than the standard compound propionaldehyde. Dichloroacetaldehyde was also found to be metabolized by this enzyme, but to a lesser extent than its monochloro-analogue. There was some evidence to suggest, however, that alcohol dehydrogenase and chloral hydrate dehydrogenase may play a significant role in the metabolism of this compound. Chloral hydrate was not metabolized by this enzyme to an appreciable extent.en_US
dc.typetexten_US
dc.typeThesis-Reproduction (electronic)en_US
dc.subjectHealth Sciences, Toxicology.en_US
dc.subjectBiology, Animal Physiology.en_US
thesis.degree.nameM.S.en_US
thesis.degree.levelmastersen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorCarter, Dean E.en_US
dc.identifier.proquest1344026en_US
dc.identifier.bibrecord.b26917452en_US
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