ラット脾臓,睾丸,胃におけるBenzylamine oxidaseの比較研究
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概要
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Using benzylamine as substrate, the existence of clorgyline- and deprenyl-resistant, but semicarbazide-sensitive amine oxidase, called benzylamine oxidase (BZO), distinct from monoamine oxidase (MAO) was established in rat spleen, testis and stomach. The proportions of BZO activity to MAO in these three preparations were extremely distinct, depending mainly on the substrate concentration used. This difference might be due to its lower Km values for benzylamine (about 3-6 μM) than those of MAO (200-250 μM), thus, at low concentrations of the substrate, it was exclusively oxidized by BZO. This amine oxidase in these preparations highly and similarly oxidized β-phenylethylamine, tyramine and tryptamine, as well as benzylamine, but its oxidations of 5-HT and dopamine were poor. It was also found here that activity was significantly inhibited by carbonyl reagents, semicarbazide and hydroxylamine and, also, by a copper-chelator, cuprizone. However, the extents of inhibition by these compounds were all similar in these three preparations tested. In addition, specific inhibitors for lysyl oxidase, β-aminopropionitrile and plasma amine oxidase, KCN, did not significantly inhibit BZO activity, indicating that this enzyme is distinct from these two pyridoxal phosphate-containing amine oxidases. From these almost identical results for comparisons of kinetics, substrate specificities and inhibitor sensitivities, this amine oxidase in rat spleen, testis and stomach appears to be identical and of one kind. However, this amine oxidase found in these organs differs from MAO, lysyl oxidase and plasma amine oxidase.
- 昭和大学・昭和医学会の論文