Isolation and Characterization of a Ferrihemeprotein Reductase from the Perienteric Fluid of Ascaris Suum
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Authors
Perdok, Monique M.
Issue Date
1992
Type
Thesis
Language
en_US
Keywords
Alternative Title
Abstract
Ascaris 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determined to be squalene (Guinn and Goldberg, unpublished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.
Description
iv, 28 p.
Citation
Publisher
Kalamazoo College
License
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