STUDIES ON MONOAMINE OXIDASE

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  • Monoamine Oxidaseに関する研究
  • Monoamine oxidaseに関する研究-10-人腎臓のMonoamine oxidaseについて
  • Monoamine oxidase ニ カンスル ケンキュウ 10 ヒト ジンゾウ ノ Monoamine oxidase ニ ツイテ
  • Report 10: Enzymic Properties of Monoamine Oxidase in Human Kidney
  • 第10報: 人腎臓のMonoamine Oxidaseについて

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Abstract

Monoamine Oxidase (MAO) [EC. 1. 4. 3. 4. monoamine: O2 oxidoreductase (deaminating) ] in human kidney was partially purified using Emulgen 810 as detergent and substrate specificity, pS and pH optimum of the purified MAO were studied. MAO activity was measured by the oxgenelectrode technique using tyramine as substrate. Enzymic activity was expressed as Qo2, which is defined as the amount of oxygen consumption (μM) per minute per mg dry weight of the enzymic preparations. The following results were obtained;<BR>1) MAO in human kindey was found mainly in mitochondrial fraction, but not in soluble fraction. These results were the same as in case of hog kindey, but the specific activity in homogenate of human kidney was lower than that of hog kidney.<BR>2) Sixty % of the mitochondrial MAO activity in human kidney was solubilized when the mitochondria was treated with the final concentration of 1% Emulgen.<BR>3) Thirty three % of MAO activity in homogenate was found in the solubilized MAO which was collected in 30% ammonium sulfate saturated solution.<BR>Purity of the enzyme was approximately 4-fold than that of in homogenate.<BR>Two hundred and twenty % of MAO activity in the solubilized fraction was found in the 15-60% ammonium sulfate saturated solution. This partially purified enzyme was relatively stable for 16 days when it was kept in freezer.<BR>4) The partially purified MAO in human kidney possessed almost the same enzymic characters as in homogenate, such as pS and pH optimum.<BR>5) The substrate specificity was studied comparing with the case of the homogenate and the purified MAO.<BR>The purified MAO oxidized tyramine, dopamine, benzylamine, phenylethylamine, tryptamine and hexylamine with fairly good velocity. However, no oxidation was observed in case of adrenaline, nor-adrenaline and serotonin in contrast with the case of homogenate. The enzymic properties of purified MAO in human kindey were almost the same as that of hog kidney, rabbit, and bovine liver.<BR>It is possible to conclude that the role and function of MAO in human tissues will be able to assume by that of experimental animals.

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