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Studies on the enzyme phenol oxidase in a freshwater monogenetic trematode

Published online by Cambridge University Press:  05 June 2009

A. Bhagavathiammai  and
K. Ramalingam
A. Bhagavathiammai
Affiliation:
Department of Zoology, University of Madras, Madras-600 055, India
K. Ramalingam
Affiliation:
Department of Zoology, University of Madras, Madras-600 055, India
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Abstract

Cytochemical localization of the enzyme phenol oxidase in Neomurraytrema tengra has been studied. Results reveal that the enzyme reacts with substrates such as catechol, hydroquinone, pyrogallol, dopa, doparmine, epinephrine and tyramine, but not with tyrosine and protocatechuic acid. Thus it shows activity with a wide range of phenols, aminated, mono and diphenols and also with deaminated and decarboxylated, di- and polyphenols. The maximum activity of the enzyme occurs between 40°C and 50°C with a pH optimum of 6–6.

Keywords

phenol oxidaseNeomurraytrema tengra
Type
Research Article
Information
Journal of Helminthology , Volume 60 , Issue 3 , September 1986 , pp. 201 - 209
Copyright
Copyright © Cambridge University Press 1986

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