Date of Award

Summer 1997

Document Type

Thesis

Degree Name

Master of Science (MS)

Department

Chemistry & Biochemistry

Program/Concentration

Chemistry

Committee Director

Patricia A. Pleban

Committee Member

Mark S. Elliot

Committee Member

Roy L. Williams

Call Number for Print

Special Collections LD4331.C45 T727

Abstract

We investigated the separation of selenoprotein P and extracellular (serum) glutathione peroxidase using a concanavalin A affinity column. We were able to show that the method does not adequately separate serum glutathione peroxidase from selenoprotein P because human glutathione peroxidase binds strongly to the column. We also found that albumin can interfere with measurement serum of glutathione peroxidase activity when hydrogen peroxide is used as the substrate. When t-butyl hydroperoxide was used as the substrate, less than 10% of the measured activity was due to the presence of albumin. We also found that the pH of the elution buffer plays an important role and that recoveries of selenium improve with increasing pH while recoveries of glutathione peroxidase activity were inversely related to the pH of the elution buffer. Based on our studies we found that this previously published method is unsuitable for estimating selenoprotein P and glutathione peroxidase levels in serum.

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DOI

10.25777/8nvk-4g44

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