Über eine neue Methode zur Bestimmung der Diaminoxydase-Aktivität

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Abstract
The ammonia released from the substrate is measured with the aid of glutamate dehydrogenase. Within wide limits, the enzyme activity is directly proportional to the amount of enzyme. The substrate concentration-activity curves with putrescine, hexamethylene diamine and benzylamine have no marked optimum, unlike those with cadaverine and histamine. The optimal concentrations for the test reaction mixture are: 0.05 ml glutamate dehydrogenase oxoglutaric acid. It was possible to show that aminoguanidine inhibits the oxidation of cadaverine more than that of histamine, and the oxidation of both substrates is strongly inhibited by semicarbazide. With the substrates cadaverine, putrescine, hexamethylene diamine, benzylamine and histamine, the diamine oxidase activity is increased up to 450% by 10-3 [image] chlorpromazine. The test system is not affected by chlorpromazine. There is good agreement between the glutamate dehydrogenase method and the o-amino-benzal-dehyde method for the measurement of diamine oxidase activity. Comparative studies show that the glutamate dehydrogenase method is also suitable for the measurement of diamine oxidase in animal tissues and in serum. It can also be used to measure other enzymatic reactions in which ammonia is produced, e.g. the determination of monoamine oxidase and urease.

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