Date of Award

Spring 1984

Document Type

Thesis

Degree Name

Master of Science (MS)

Department

Chemistry & Biochemistry

Program/Concentration

Chemistry

Committee Director

James H. Yuan

Committee Member

Patricia A. Pleban

Committee Member

Robert L. Ake

Call Number for Print

Special Collections LD4331.C45L57

Abstract

Investigation of the coenzyme binding site of lactate dehydrogenase was approached by using coenzyme analogs. Inhibition studies of this enzyme using n-alkylphosphates as coenzyme analogs were performed with a fluorometric method. The results showed that all of the n-alkylphosphates were competitive inhibitors with respect to NAD+.

The n-alkyl-ADPs were synthesized from AMP and dicycloheaylammonium salts of n-alkylphosphates. The synthetic compounds were subjected to NMR spectroscopic studies, thin layer chromatography and determination of the ratio of adenosine moiety to phosphate groups. The results indicated that the synthetic compounds were n-alkyl-ADPs.

These synthetic compounds were used as coenzyme analogs in inhibition studies of lactate dehydrogenase. The results showed that all were competitive inhibitors. Inhibitor dissociation constants of both series of inhibitors were calculated from the experimental data. The inhibitor dissociation constants of all of the n-alkyl-ADPs were at least ten times smaller than those of their corresponding n-alkylphosphates. This indicated that the stronger binding effect is due to AMP moiety.

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DOI

10.25777/jt33-5j44

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