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Kinetic and electrophoretic studies on acid and alkaline phosphatases of the metacercariae of Clinostomum complanatum (Trematoda: Digenea)

Published online by Cambridge University Press:  18 November 2009

Afzal A. Siddiqui  and
Wajih A. Nizami
Afzal A. Siddiqui
Affiliation:
Section of Parasitology, Department of Zoology, Aligarh Muslim University, Aligarh-202001, India
Wajih A. Nizami
Affiliation:
Section of Parasitology, Department of Zoology, Aligarh Muslim University, Aligarh-202001, India
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Abstract

Homogenates of the metacercariae of Clinostomum complanatum showed two peaks for the hydrolysis of p-nitrophenyl phosphate at pH 4·5–5·0 and 11·0; specific activity at pH 5·0 was 0·017 µmol p-nitrophenol/mg protein/min and 0·0049 µmol p-nitrophenol/mg protein/min at pH 11·0 at 37°C. Maximal activities of acid and alkaline phosphatases were observed at 50° and 40°C respectively. Both enzymes reached maximal rates after 50 min of incubation. Linearity in enzyme activity was noticed with increasing homogenate concentrations for both enzymes. The Km for p-nitrophenyl phosphate was 1·1 mM with a Vmax of 0·018 units/mg protein for acid phosphatase and 1·6 mM with a Vmax of 0·0052 units/mg protein for alkaline phosphatase. Sodium arsenate and sodium fluoride inhibit and Mg++ and Co++ stimulate both enzymes. Polyacrylamide gel electrophoresis showed one cathodic band each for both the enzymes.

Type
Research Papers
Information
Journal of Helminthology , Volume 56 , Issue 1 , March 1982 , pp. 17 - 22
Copyright
Copyright © Cambridge University Press 1982

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