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Science 18 December 1992:
Vol. 258. no. 5090, pp. 1930 - 1932
DOI: 10.1126/science.1470914

Articles

Science, Vol 258, Issue 5090, 1930-1932
Copyright © 1992 by American Association for the Advancement of Science


articles

Components of sterol biosynthesis assembled on the oxygen-avid hemoglobin of Ascaris

DR Sherman, B Guinn, MM Perdok, and DE Goldberg

Department of Medicine, Washington University School of Medicine, St. Louis, MO.

The parasitic nematode Ascaris infests a billion people worldwide. Much of its proliferative success is due to prodigious egg production, up to 10(6) sterol-replete eggs per day. Sterol synthesis requires molecular oxygen for squalene epoxidation, yet oxygen is scarce in the intestinal folds the worms inhabit. Ascaris has an oxygen-avid hemoglobin in the perienteric fluid that bathes its reproductive organs. Purified hemoglobin contained tightly bound squalene and functioned as an NADPH-dependent, ferrihemoprotein reductase. All components of the squalene epoxidation reaction--squalene, oxygen, NADPH, and NADPH-dependent reductase--are assembled on the hemoglobin. This molecule may thus function in sterol biosynthesis.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Nonvertebrate Hemoglobins: Functions and Molecular Adaptations.
R. E. Weber and S. N. Vinogradov (2001)
Physiol Rev 81, 569-628
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Science. ISSN 0036-8075 (print), 1095-9203 (online)