Characterization of mitochondrial monoamine oxidase of Ascaridia galli

Oxidative deamination of various biogenic monoamines by Ascaridia galli monoamine 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 inhibi...

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Bibliographic Details
Published inJournal of helminthology Vol. 59; no. 2; pp. 101 - 107
Main Authors Mishra, S.K, Agarwal, A, Sen, R, Ghatak, S
Format Journal Article
LanguageEnglish
Published England 01.06.1985
Subjects
amine oxidase (flavin-containing)
Animals
Ascaridia - enzymology
Ascaridia galli
enzyme inhibitors
mitochondria
Mitochondria - enzymology
Monoamine Oxidase - analysis
Monoamine Oxidase Inhibitors - pharmacology
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Summary:Oxidative deamination of various biogenic monoamines by Ascaridia galli monoamine 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 (8 microM) and Ki (12 microM) values. Chlorgyline and deprenyl at 100 microM concentration inhibited MAO by about 60 and 40% respectively, indicating the presence of both type A and type B MAO in A. galli.
ISSN:0022-149X
1475-2697
DOI:10.1017/S0022149X00025669