Effects of hydroxylamine on mitochondrial monoamine oxidase in rat liver
| Autor: | Kazuya Kamijo, Takako Watanabe |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
Male
chemistry.chemical_classification Tryptamine Benzylamines Monoamine oxidase Tyramine Mitochondria Liver General Chemistry General Medicine Hydroxylamines Rats Kinetics chemistry.chemical_compound Enzyme Hydroxylamine Monoamine neurotransmitter Benzylamine chemistry Biochemistry Hexylamine Drug Discovery Animals Female Monoamine Oxidase |
| Zdroj: | Chemical and Pharmaceutical Bulletin. 24:698-704 |
| ISSN: | 1347-5223 0009-2363 |
| Popis: | The report here is the study as for the effects of NH2OH on the enzymic reaction of monoamine oxidase (MAO) using rat liver mitochondria. In the short-term reaction (1 min) by MAO, NH2OH decreased the MAO activity by either tyramine or benzylamine as substrate. In the long-term reaction (60 min), there was an increased activity in the MAO reaction by tyramine and an decreased one in that by benzylamine under various concentrations of NH2OH. In the long-term reaction, Km-values for tyramine and benzylamine were 1.82×10-3.0M and 2.50×10-2.0M, respectively, which were consistent with those in the presence of NH2OH. Pursuing the changes of MAO activities by various concentrations of NH2OH using the tyramine substrate at intervals of 1, 10, 30, and 60 min, there was a decrease of MAO activity accompanying an increased concentration of NH2OH after 1 min period, a partial increase after 10 min, and an entire increase in extensive concentrations of NH2OH after 30 min. In the other substrates such as tryptamine, amylamine, hexylamine, and β-phenylethylamine, the effects of NH2OH on MAO were similar to those in tyramine. In the butylamine substrate, NH2OH caused as inhibitory effects as shown in the benzylamine substrate. These results suggest the existence of a complex of MAO enzymes corresponding to monoamine substrates. The multiplicity of MAO enzyme is further discussed in the text. |
| Databáze: | OpenAIRE |
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