NDLI: Reactivity of liver monoamine oxidase in the seal Phoca hispida ladogensis

Content Provider	Springer Nature Link
Author	Basova, I. N. Yagodina, O. V.
Copyright Year	2013
Abstract	The goal of this work consisted in substrate and inhibitor specificity of liver monoamine oxidase (MAO) of the freshwater Ladoga subspecies of the ringed seal Phoca hispida ladogensis. The studied enzyme has been found to have the large substrate specificity by deaminating, apart from eight classic substrates of the terrestrial mammalian MAO, also histamine, the substrate of diamino oxidase. It has been revealed that the studied enzyme realizes wide substrate specificity by deaminating, apart from eight classic MAO substrates of terrestrial mammals, also histamine, the substrate of diamino oxidase. The deamination rates of benzylamine, β-phenylethylamine, and N-methylhistamine are found to be almost by one order higher than the deamination rates of serotonin and noradrenaline. The seal liver MAO did not deaminate putrescine and cadaverine and was insensitive to 10$^{−2}$ M semicarbaside. There were calculated bimolecular rate constants of interaction of inhibitors: chlorgyline, deprenyl, berberine, sanguinarine, chelidonine, and four derivatives of acridine with the enzyme at deamination of nine substrates. By the method of substrate-inhibitor analysis we have shown heterogeneity of the enzyme, i.e., the presence in the seal liver of at least of two different MAO.
Starting Page	138
Ending Page	144
Page Count	7
File Format	PDF
ISSN	00220930
Journal	Journal of Evolutionary Biochemistry and Physiology
Volume Number	49
Issue Number	2
e-ISSN	16083202
Language	English
Publisher	SP MAIK Nauka/Interperiodica
Publisher Date	2013-06-08
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	monoamine oxidase monoamines liver seal Evolutionary Biology Biochemistry Animal Physiology
Content Type	Text
Resource Type	Article
Subject	Physiology Biochemistry Ecology, Evolution, Behavior and Systematics

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