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Acid phosphatase activity demonstrated by intact Angiostrongylus cantonensis with special reference to its function

Published online by Cambridge University Press:  06 April 2009

Jun Maki  and
Toshio Yanagisawa
Jun Maki
Affiliation:
Department of Parasitology, School of Medicine, Kitasato University, Sagamihara, Kanagawa Prefecture, Japan
Toshio Yanagisawa
Affiliation:
Department of Parasitology, School of Medicine, Kitasato University, Sagamihara, Kanagawa Prefecture, Japan
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Summary

Intact Angiostrongylus cantonensis is able to hydrolyse glucose-phosphate esters, mononucleotides and p-nitrophenyl phosphate as well as β-glycerophosphate in vitro. Reciprocal inhibition studies suggest that the hydrolysis of such substrates is due to a non-specific phosphomonoesterase. Molybdate ions, which exert no effect on either the uptake of glucose or the production of lactate, inhibit the hydrolysis of glucose-1- phosphate in the external medium and simultaneously lower the production of lactate by the intact worms in vitro.

Type
Research Article
Information
Parasitology , Volume 79 , Issue 3 , December 1979 , pp. 417 - 423
Copyright
Copyright © Cambridge University Press 1979

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