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Characterization of mitochondrial monoamine oxidase of Ascaridia galli

Published online by Cambridge University Press:  18 November 2009

S.K. Mishra ,
Abha Agarwal ,
Ramanuj Sen  and
S. Ghatak
S.K. Mishra
Affiliation:
Division of Biochemistry, Central Drug Research Institute, Lucknow-226001, India
Abha Agarwal
Affiliation:
Division of Biochemistry, Central Drug Research Institute, Lucknow-226001, India
Ramanuj Sen
Affiliation:
Division of Biochemistry, Central Drug Research Institute, Lucknow-226001, India
S. Ghatak
Affiliation:
Division of Biochemistry, Central Drug Research Institute, Lucknow-226001, India
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Abstract

Oxidative deamination of various biogcnic monoamines by Ascaridia galli monoaminc oxidase (MAO) was blocked by different mammalian MAO inhibitors, namely, iproniazid, trans-PcP, nialamide and pargyline and the blockade was observed to be time as well as concentration dependent. The binding of inhibitors with chick ascarid MAO was of the irreversible type and the nature of the inhibition was competitive. Pargyline showed lowest I50 (8µM) and K1 (12µM) values. Chlorgyline and deprenyl at 100µM concentration inhibited MAO by about 60 and 40% respectively, indicating the presence of both type A and type B MAO in A. galli.

Type
Research Article
Information
Journal of Helminthology , Volume 59 , Issue 2 , June 1985 , pp. 101 - 107
Copyright
Copyright © Cambridge University Press 1985

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