Isolation and Characterization of a Ferrihemeprotein Reductase from the Perienteric Fluid of Ascaris Suum

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dc.contributor.advisorGoldberg, Daniel
dc.contributor.authorPerdok, Monique M.
dc.descriptioniv, 28 p.en_US
dc.description.abstractAscaris suum, an intestinal parasite of the pig, has a perienteric hemoglobin with an affinity for oxygen approximately 25,000 times greater than that of human hemoglobin. With such a high oxygen affinity, it does not appear probable that the hemoglobin delivers oxygen to the tissues of the organism at a significant rate. Purification of the hemoglobin revealed an associated factor which was determined to be squalene (Guinn and Goldberg, unpublished data) . Squalene is an intermediate in the cholesterol biosynthetic pathway and requires molecular oxygen and a NADPH-dependent reductase for conversion to squalene epoxide. This led to the proposal that the hemoglobin in A. suum is an enzyme that acts in cholesterol biosynthesis. was purified and a colormetric assay was The hemoglobin employed to investigate its enzymatic characteristics including V mas, K m, temperature optimum, and pH optimum. It was determined that the perienteric hemoglobin A. suum can reduce oxidized cytochrome c (and possibly other ferrihemeproteins) in an NADPH-dependent fashion supporting the working hypothesis that the hemoglobin is an enzyme involved in cholesterol biosynthesis.en_US
dc.description.sponsorshipDepartment of Molecular Microbiology. Washington University. St. Louis, Missouri.
dc.publisherKalamazoo Collegeen_US
dc.relation.ispartofKalamazoo College Biology Senior Individualized Projects Collection
dc.relation.ispartofseriesSenior Individualized Projects. Biology;
dc.rightsU.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder.
dc.titleIsolation and Characterization of a Ferrihemeprotein Reductase from the Perienteric Fluid of Ascaris Suumen_US