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dc.contributor.advisorCraney, Chris
dc.contributor.authorOvanessian, Jason
dc.date.accessioned2020-08-13T14:55:10Z
dc.date.available2020-08-13T14:55:10Z
dc.date.issued2002-01-01 0:00
dc.identifier.urihttps://scholar.oxy.edu/handle/20.500.12711/284
dc.description.abstractGlucose-6-Phosphate Dehydrogenase (G6PD) catalyzes the first step in the Pentose Phosphate Pathway by oxidizing glucose-6-phosphate (G6P) to 6-phosphogluconolactone. Simultaneously, nicotinamide adenine dinucleotide phosphate (NADP<sup>+</sup>) is reduced to NADPH. Through this reaction, G6PD maintains adequate levels of NADPH within cells. The NADPH in turn, is used for protection against oxidative damage, especially within erythrocytes, or red blood cells. By using High Performance Liquid Chromatography (HPLC), large zone elution profiles for the molecular weight standards Bovine Serum Albumin (BSA) and a-Amylase were obtained. Large zone elution profiles for G6PD were also obtained. Through integration in Graphical Analysis, centroid elution times were determined using the trapezoid method. Results obtained from previous experiments show that by lowering the enzyme concentration through serial dilution, the dissociation of the G6PD dimer to a monomer is encouraged. However, at an absorbance range of 280 nm, such a low concentration of G6PD (&lt; 1.2 x 10<sup>-9</sup> mol/L) makes it difficult to distinguish signal from background noise. Current studies are aimed at determining which increased Potassium Chloride (KCl) concentrations will encourage the dimer dissociation at higher enzyme concentrations. It is our goal to determine the monomer-dimer equilibrium and to calculate KD.
dc.description.sponsorshipNational Science Foundation-Research Experience for Undergraduate Grant
dc.titleGlucose-6-Phosphate Dehydrogenase (G6PD) Association Studies
dc.typearticle
dc.abstract.formathtml
dc.description.departmentbiochem
dc.source.issueurc_student
dc.source.issueurc_student
dc.identifier.legacyhttps://scholar.oxy.edu/urc_student/135
dc.source.statuspublished


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