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Phosphatase systems in Fasciolopsis buski Lankester, 1857 and Gastrodiscus aegyptiacus Cobbold, 1876

Published online by Cambridge University Press:  06 April 2009

Madan M. Goil
Madan M. Goil
Affiliation:
Department of Zoology, Bareilly College, Bareilly, U.P., India
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Extract

Biochemical studies on the non-specific phosphomonoesterases have demonstrated the presence of acid phosphomonoesterase with maximum activity at pH 4·0 in Gastrodiscus aegyptiacus (enzyme I) and at pH 4·5 in the case of Fasdolopsis buski (enzyme II). The Km for ρ-nitrophenyl phosphate hydrolysis was 0·66 mM for enzyme I and 1·1 mM for enzyme II. Different concentrations of fluoride, arsenate, tartrate, tartaric acid, cysteine and copper brought about inhibition of both enzymes and magnesium, iodoaeetate, iodoacetamide and EDTA had no influence on either enzyme activity. Cobalt activated both enzymes while zinc inhibited enzyme I and strongly stimulated enzyme II.

Type
Research Article
Information
Parasitology , Volume 67 , Issue 2 , October 1973 , pp. 197 - 204
Copyright
Copyright © Cambridge University Press 1973

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References

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