Chemistry ETDs

Publication Date

1-20-1978

Abstract

The role of the metal ion in rat erythrocyte glyoxalase I was evaluated. The apoenzyme was formed by dialysis against an EDTA-imidazole buffer. Fluorescence studies of the Mg++- and Mn++-dansylated glyoxalase I's suggest that the metal ion is near the active site of the enzyme and participates in the catalytic reaction. Stereochemical studies of the conversion of methylglyoxal to S-lactoylglutathione with Mg++, Mn++, Co++ and Ni++-glyoxalase I's show that the 0-lactate of S-lactoylglutathione (97±1.5%) is formed. This result suggests that the reaction mechanism is the same with a change in metal ion.

Language

English

Document Type

Dissertation

Degree Name

Chemistry

Level of Degree

Doctoral

Department Name

Department of Chemistry and Chemical Biology

First Committee Member (Chair)

David Vander Jagt

Second Committee Member

William Fletcher Coleman

Third Committee Member

Unknown

Fourth Committee Member

Philip Reyes

Fifth Committee Member

Unknown

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