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Comparative enzymologic study of catalytical properties of liver monoamine oxidases of sturgeon fish

  • Comparative and Ontogenic Biochemistry
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Abstract

We carried out the comparative study of the substrate and inhibitory specificity of liver monoamine oxidases (MAO) of the giant sturgeon Huso huso, the starred sturgeon Acipenser stellatus, the Persian sturgeon Acipenser persicus, and the Russian sturgeon Acipenser gueldenstaedtii. Results of the substrate-inhibitor analysis with use of inhibitors chlorgilin and deprenil, as well as five specific substrates indicate homogeneity of these enzymes. All studied MAO have the several orders higher sensitivity to chlorgilin than to deprenil, with essential interspecies differences being observed. There are determined kinetic parameters of enzymatic deamination (K M and V) of tyramine, serotonin, noradrenalin, benzylamine, β-phenylethylamine, and N-methylhistamine. All studied enzymes have been established to have the higher activity toward serotonin and noradrenalin-substrates of the MAO A form as compared with benzylamine, β-phenylethylamine, and N-methylhistamine-substrate of the mammalian MAO B form, the maximal activity being characteristic of the giant sturgeon.

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Authors and Affiliations

  1. Sechenov Institute of Evolutionary Physiology and Biochemistry, Russian Academy of Sciences, St. Petersburg, Russia

    O. V. Yagodina & I. N. Basova

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  1. O. V. Yagodina
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  2. I. N. Basova
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Correspondence to O. V. Yagodina.

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Original Russian Text © O.V. Yagodina, I.N. Basova, 2013, published in Zhurnal Evolyutsionnoi Biokhimii i Fiziologii, 2013, Vol. 49, No. 3, pp. 203–210.

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Yagodina, O.V., Basova, I.N. Comparative enzymologic study of catalytical properties of liver monoamine oxidases of sturgeon fish. J Evol Biochem Phys 49, 300–308 (2013). https://doi.org/10.1134/S0022093013030043

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  • DOI: https://doi.org/10.1134/S0022093013030043

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