Abstract
Glucose-6-phosphate dehydrogenase (G6PD) catalyzes the first step in the pentose phosphate pathway by converting glucose-6-phosphate to 6-phosphogluconolactone. During this rate-limiting step, nicotinamide adenine dinucleotide phosphate (NADP+) is reduced to NADPH. Cells, in particular human erythrocytes, rely on the NADPH generated by this reaction for protection against oxidative damage. By using high performance liquid chromatography (HPLC), small zone elution profiles for the molecular weight standards bovine serum albumin and beta-amylase were obtained. Small zone elution profiles for G6PD were also obtained. Through analysis in Microsoft Excel, the retention time and elution volume for each run was determined. Current studies involving HPLC are aimed at determining which potassium iodide concentrations will encourage the G6PD dimer to dissociate to its monomer form. From this information, it is hoped that the monomer-dimer equilibrium for G6PD can be determined.
