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Characterization of phenol oxidase in a pseudophyllidean cestode Penetrocephalus ganapatii

Published online by Cambridge University Press:  06 April 2009

C. Jayabaskaran  and
K. Ramalingam
C. Jayabaskaran
Affiliation:
Department of Zoology, University of Madras, Madras-600 005, India
K. Ramalingam
Affiliation:
Department of Zoology, University of Madras, Madras-600 005, India
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Extract

The biochemical characteristics of phenol oxidase obtained from Penetrocephalus ganapatii have been investigated using manometric and electrophoretic techniques. Phenol oxidase was found to have maximum activity at pH 7·4, the Michaelis constant for dopamine was 189 μM and the enzyme was stable between 20 and 40°C. Potassium cyanide, sodium diethyldithiocarbamate and phenylthiourea strongly suppressed enzyme activity. The Ki values for potassium cyanide, diethyldithiocarbamate and phenylthiourea were 33μM, 700 μM and 938 μM respectively. The properties of soluble and insoluble enzymes to various phenolic substrates are discussed.

Information

Type
Research Article
Information
Parasitology , Volume 90 , Issue 3 , June 1985 , pp. 433 - 440
Copyright
Copyright © Cambridge University Press 1985

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