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Studies on glucose-6-phosphate dehydrogenase from the human parasite, Onchocerca volvulus

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Abstract

Glucose-6-phosphate dehydrogenase (E.C. 1.1.1.49) was partially purified from the extracts of adult Onchocerca volvulus by affinity chromatography on 2′5′ADP-Sepharose-4B. Kinetic studies revealed a typical bell-shaped pH profile with an optimum lying between pH 7.3 and 7.8. The apparent Km for glucose-6-phosphate was 5.66×10−5 M, whereas that for NADP was 2.17×10−6 M. Suramin, a filaricidal drug, inhibited the enzyme competitively with respect to NADP as a substrate: the apparent Ki values were 2.23×10−6 M and 4.21×10−7 M, respectively, for the crude and purified enzyme preparations. Glucose-6-phosphate dehydrogenase therefore, could be one of the targets of suramin in vivo.

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Authors and Affiliations

  1. Biochemistry Service, Box 812, Faculty of Science, University of Yaoundé, Yaoundé, Cameroon

    Vincent P. K. Titanji, John-Payne Muluh & Jean-Roger Tchoupe

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  1. Vincent P. K. Titanji
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  2. John-Payne Muluh
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  3. Jean-Roger Tchoupe
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Titanji, V.P.K., Muluh, JP. & Tchoupe, JR. Studies on glucose-6-phosphate dehydrogenase from the human parasite, Onchocerca volvulus . Parasitol Res 74, 380–382 (1988). https://doi.org/10.1007/BF00539461

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  • DOI: https://doi.org/10.1007/BF00539461

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