Substrate specificity of rat liver aldehyde dehydrogenase with chloroacetaldehydes
AdvisorCarter, Dean E.
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PublisherThe University of Arizona.
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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.
Degree ProgramGraduate College
Pharmacology & Toxicology