I. N. Basova

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There has been carried out a study of substrate and inhibitor specificity of the liver mitochondrial monoamine oxidase (MAO) of the striped-bellied tunny Katsuwonus pelamis. Results of the substrate-inhibitor analysis with use of chlorgilin and deprenyl are an indirect proof for the existence in the tunny liver of one molecular MAO form. The studied enzyme,(More)
There is performed a comparative analysis of action of four acridine derivatives and of one xanthene derivative (pyronin G) on activity of liver monoamine oxidase (MAO) of two species of poikilothermal freshwater animals: a representative of amphibians—the common frog Rana temporaria and a representative of the Salmonidae order—the European whitefish(More)
99 Monoamine oxidase (MAO, EC 1.4.3.4) is the key enzyme of metabolism of neurotransmitters and other biogenic amines. The majority of studies have been performed with MAO of have terrestrial mammals, whose liver contains two forms of this enzyme—MAO A and MAO B [1, 2]. According to modern knowledge, serotonin is deaminated by MAO A; benzylamine, by MAO B;(More)
Study of substrate-inhibitory specificity of liver mitochondrial monoamine oxidase (MAO) of adult individuals of the whitefish Coregonus lavaretus ludoga P. from the Ladoga Lake has revealed distinguished peculiarities of catalytic properties of this enzyme. The studied MAO, on one hand, like the classical enzyme of homoiothermal animals, is able to(More)
247 Monoamine oxidase (MAO; monoamine:O 2 oxidoreductase (deaminating); EC 1.4.3.4) is a membranebound widespread thiol enzyme that catalyzes the reaction of oxidative deamination of biogenic amines. It is contained in almost all organs of humans and mammals. Homologous enzymes were found in plants, microorganisms, and invertebrates [1]. The majority of(More)
56 To date, the catalytic properties of monoamine oxidase (MAO; monoamine: é 2 oxidoreductase (deaminating); EC 1.4.3.4) have been studied mostly in representatives of mammals. Fish MAO have been poorly studied. According to the published data, this enzyme exhibits highly diverse properties both in quantitative (specific activity) and qualitative(More)
270 The substrate-inhibition specificity of liver monoamine oxidase (MAO) has been studied in mature lampreys ( Lampetra fluviatilis ) of both sexes. The catalytic properties of the enzyme have been found to resemble those of the classic mammalian MAO: the enzyme deaminates tyramine, tryptamine, serotonin, and benzylamine, but not histamine; it is sensitive(More)
Study of the substrate-inhibitory specificity of mitochondrial monoamine oxidase (MAO) of hepatopancreas of the octopus Bathypolypus arcticus revealed distinctive peculiarities of catalytic properties of this enzyme. The studied enzyme, on one hand, like the classic MAO of homoiothermal animals, is able to deaminate tyramine, serotonin, benzylamine,(More)
148 In recent years, the interest to designing new therapeutic and prophylactic tools of plant origin, including those from coniferous plants, which contain a broad spectrum of biologically active compounds, has considerably increased [1]. Modern technologies make it possible to isolate and concentrate biologically active compounds from plant row materials,(More)
Comparative enzymological study of catalytical properties of monoamine oxidase (MAO) of liver of the marsh frog Rana ridibunda and common frog Rana temporaria has revealed certain features of similarity and differences between these enzymes. The MAOs from both studied biological sources show catalytic properties resembling those of the classical MAO of(More)