Abstract: Aldehyde dehydrogenase is a polymorphic enzyme responsible for the oxidation of aldehydes to carboxylic acids, which leave the liver and are metabolized by the body’s muscle and heart. This study aimed at investigating the number of sulfhydryl groups present in aldehyde dehydrogenase. Urea Polyacrylamide Gel Electrophoresis (Urea-PAGE) approach was used to count the integral number of sulfydryl groups present in Bakers‘ yeast aldehyde dehydrogenase. Aldehyde dehydrogenase solution was sequentially denatured, reduced and alkylated using urea, dithiothreitol (DTT), iodoacetamide and iodoacetic acid solutions. This was subsequently analysed on 8.0 M Urea-PAGE at 100 v for 4 hours and stained by fast Coomassie method. A single band on the 8.0 M Urea-PAGE indicates that the enzyme, aldehyde dehydrogenase, contains one disulfide bond. This disulfide bond present in the enzyme might contribute to the stability of the enzyme.
Keywords: Aldehyde dehydrogenase, Urea-PAGE, Bakers‘yeast, disulfide, stability.
Title: Counting the Integral Number of Sulfhydryl Groups in Bakers’ Yeast Aldehyde Dehydrogenase Using Urea-Polyacrylamide Gel Electrophoresis
Author: Mojisola Ojebode
International Journal of Thesis Projects and Dissertations (IJTPD)
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