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Partial purification and characterization of a soluble acid phosphatase from the tapeworm, Hymenolepis diminuta

Published online by Cambridge University Press:  05 June 2009

Michael J. Bumbulis  and
Peter W. Pappas
Michael J. Bumbulis
Affiliation:
Department of Zoology, The Ohio State University, Columbus, OH 43120–1293, USA
Peter W. Pappas*
Affiliation:
Department of Zoology, The Ohio State University, Columbus, OH 43120–1293, USA
*
*To whom correspondence should he addressed
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Abstract

An acid phosphatase activity (APA; EC 3.1.3.2) was demonstrated in homogenates of adult Hymenolepis diminuta. The APA was soluble based on the observation that it did not sediment at 130 000 g. APA was partially purified using a combination of differential centrifugation, ammonium sulphate precipitation, chloroform extraction, and gel and fast-protein-liquid-chromatography. This combination of techniques resulted in a preparation with a specific activity approximately 500 times greater than the crude enzyme preparation. The temperature and pH optima of the partially purified APA were 44°C and pH 5·0. The enzyme appeared to be a monomer with a molecular weight of approximately 62 000. APA had a higher affinity for a greater activity towards aromatic than aliphatic phosphoesters and phosphoryl transferase activity was demonstrable using 1-butanol and ethylene glycol as acceptors. APA was inhibited significantly by sodium dodecyl sulphate, fluoride, molybdate and tartrate, but CuSO4 and Fast Garnet GBC were poor inhibitors. The precise cellular localization and function of this enzyme remains unknown since it possesses characteristics of both cytoplasmic and lysosomal APA's of other organisms.

Keywords

Hymenolepis diminutaCestodaacid phosphatasephosphoryl transferasetartratefluoride
Type
Research Papers
Information
Journal of Helminthology , Volume 65 , Issue 2 , June 1991 , pp. 103 - 110
Copyright
Copyright © Cambridge University Press 1991

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