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Activation and inhibition of the brush-border membrane-bound alkaline phosphatase activity of Hymenolepis diminuta (Cestoda) by divalent cations

Published online by Cambridge University Press:  06 April 2009

P. W. Pappas
P. W. Pappas
Affiliation:
The Department of Zoology, The Ohio State University, Columbus, OH 43210, USA
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Summary

In the absence of exogenous divalent cations, the isolated brush-border plasma membrane of Hymenolepis diminuta possesses alkaline phosphatase activity (APA). APA is stimulated in the presence of exogenous Mg2+ and inhibited by low concentrations of Zn2+ or high concentrations of Ca2+, and inhibition of APA by Zn2+ is reversed by both Mg2+ and Ca2+. APA is inhibited by ethylenediamine tetraacetic acid (EDTA), ethyleneglycol-bis-(β-aminoethyl ether) N, N′-tetraacetic acid, and 1, 10-phenanthroline in time- and concentration-dependent fashions, with EDTA being the most effective inhibitor. Following treatment with EDTA, APA is restored by Mg2+ and, to a lesser extent, by Ca2+, but not by Zn2+. Thus, APA represents a Mg2+-dependent enzyme that can be partly activated by Ca2+ but only in the absence of Mg2+.

Keywords

Hymenolepis diminutamembrane-bound enzymealkaline phosphatasebrush-border membranetegumentmagnesiumcalciumzincEDTAEGTAo-phenanthroline
Type
Research Article
Information
Parasitology , Volume 102 , Issue 1 , February 1991 , pp. 141 - 145
Copyright
Copyright © Cambridge University Press 1991

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