Catalytic characteristics of monoamine oxidase of whitefish Coregonus lavaretus ludoga

Basova, I. N.; Yagodina, O. V.

doi:10.1134/s0022093011040025

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“…It is to be noted that the capability for inhibition under effect chlorgilin in the sturgeon liver MAO turned out to be several orders higher, while under action of deprenil-virtually the same as in the whitefish liver MAO [13]. The fish MAO sensitivity to inhibitors has been shown to have pronounced species specificity and to be unique in its nature, by differing from sensitivity of the enzyme of terrestrial mammals.…”

Section: Resultsmentioning

confidence: 98%

“…The revealed in this work absence of specific action of each of inhibitors at deamination of different substrates is an indirect evidence for the presence in liver MAO of the studied sturgeon fish of one substrate binding center or one molecular enzyme form. It is to be noted that earlier, by the method of the substrate-inhibitor analysis, we also showed the "kinetic" homogeneity of liver MAO of other bony fish: the European whitefish Coregonus ludoga [13], chum Oncorhynchus keta [14], and striped tuna Katsuwonus pelamis [15].…”

Section: Resultsmentioning

confidence: 99%

“…Since the performed substrate-inhibitor analysis with use of chlorgilin and deprenil indicated homogeneity of the studied enzymes, we determined kinetic parameters of enzymatic reactions of deamination of several substrates ( Table 2). The set of used substrates included both six classic MAO [13] has become the ground for its use as a possible substrate in the presented work. The studied enzymes have been established to deaminate tyramine, serotonin, noradrenaline, benzylamine, PEA, and N-methylhistamine, with no deamination of histamine.…”

Section: Resultsmentioning

confidence: 99%

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

Yagodina

Basova

2013

J Evol Biochem Phys

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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. and by predominant oxidation of substrates [1]. MAO, like other membrane-bound enzymes, are difficult to be isolated in a poor state; therefore, the substrate and inhibitor analyses are extremely convenient way of study of catalytical properties of this enzyme. Among the majority of MAO, of particular importance is enzyme of fish organs and tissues owing to an expressed peculiarity of its substrate and inhibitor characteristics. Based on results of the substrate-inhibitor analysis, a suggestion is put forward about the presence in liver and brain of the fish paku Piaractus mesopotamicus Holmberg [2], goldfish Carassius auratus L. [3], and the sheatfish Parasilus asotus [4] of one MAO form similar with the MAO A form of terrestrial mammals, while in liver of carp Cyprinidae [5], the rainbow trout Salmo gairdneri [6], and the zebrafish Danio rerio [7]-about the presence

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Section: Resultsmentioning

confidence: 98%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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