Ethanol metabolism by the mixed function oxidase system / by Thomas Richard Ward.

Author/creator Ward, Thomas R. author.
Other author Pennington, Sam N., degree supervisor.
Other author East Carolina University. Department of Biology.
Format Theses and dissertations
Production1972.
Description53 leaves : illustrations ; 28 cm
Supplemental ContentAccess via ScholarShip
Subjects

Summary Ethanol is oxidized into acetaldehyde by the enzyme alcohol dehydrogenase utilizing the cofactor NAD, but this system is not affected by chronic exposure to ethanol. Recently the microsomal fraction of the hepatic parenchymal cells along with NADPH and molecular oxygen has been shown to oxidize ethanol in vitro. In this study it was shown that the microsomal system is active in ethanol oxidation vivo, and that this system is induced by chronic ethanol consumption. To study the microsomal ethanol oxidase system, pyrazole was used to inhibit alcohol dehydrogenase vivo. Because there was no method of detecting pyrazole in whole blood a method was developed for this purpose. The microsomal ethanol oxidase system was further studied by solubilizing the microsomes and separating the component parts using a DEAE cellulose anion exchange column. It was found that NADPH cytochrome P-450 reductase, cytochrome P-450, a hydrogen peroxide generating factor (possibly dismutase), and catalase or peroxidase to utilize the hydrogen peroxide are all needed for the oxidation of ethanol into acetaldehyde by the microsomes.
General noteSubmitted to the faculty of the Department of Biology.
General noteAdvisor: Sam N. Pennington
Dissertation noteM.A. East Carolina University 1972
Bibliography noteIncludes bibliographical references (leaves 47-50).
Genre/formdissertations.
Genre/formAcademic theses.
Genre/formAcademic theses.
Genre/formThèses et écrits académiques.

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