Multiplicity of monoamine oxidase in chick brain.

The substrate- and inhibitor-related characteristics of monoamine oxidase (MAO) were studied on chick brain mitochondria. It was found that neither 5-hydroxytryptamine nor beta-phenylethylamine is the specific substrate for type A and type B MAO in chick brain.     

Cadmium-induced inhibition of brain monoamine oxidase in the freshwater catfish

Summary The freshwater catfishClarias batrachus (L.), exposed to 50 ppm of cadmium (Cd) chloride for a period of 135 days exhibited marked inhibition of brain monoamine oxidase (MAO) (p<0.001). The retarded gonadal growth observed in the present study suggests that Cd may be capable of creating imbalance in the aminergic activity of the hypothalamus, which modulates the secretion and release of gonadotropins.Acknowledgment. Financial assistance from the Council of Scientific and Industrial Research of India made this work possible.     

Identification of flavin in the purified beef brain mitochondrial monoamine oxidase

Zusammenfassung Die Monoaminoxydase in den Mitochondrien des Rinderhirns wurde gereinigt. FAD wurde durch Fluoreszenzspektrum und Dünnschichtchromatographie als prosthetische Gruppe in den gereinigten Präparaten identifiziert.     

Effect of iproniazid on monoamines and monoamine oxidase in human brain

Zusammenfassung Iproniazid in therapeutischen Dosen verursacht beim Menschen eine ausgesprochene Hemmung der Gehirn-Monoaminoxidase und eine Verdoppelung des Gehalts an 3-Hydroxytyramin, Nor-adrenalin und 5-Hydroxytryptamin.     

The stimulation of rat brain monoamine oxidase by dietary lithium chloride

Summary Lithium chloride administered to rats in drinking water for 30 days caused an increase of whole brain monoamine oxidase specific activity to approximately 140% of control. Carboxylesterase and formyltetrahydrofolate synthetase activities were not affected by Li⁺ either in vivo or in vitro.Contribution of the Nevada Agricultural Experiment Station (Reno), Journal Series No. 439.     

Histochemical remarks on monoamine oxidase and acetylcholinesterase in some regions of amphibian brain

Summary The histochemical localization of monoamine oxidase and acetylcholinesterase has been studied in the cerebellum, optic tectum and telencephalon of three amphibian species. For acetylcholinesterase in particular, different histochemical methods and selective inhibitors have been used in order to investigate the actual nature of enzymatic activity revealed.     

The stimulation of rat brain monoamine oxidase by dietary lithium chloride.

Lithium chloride administered to rats in drinking water for 30 days caused an increase of whole brain monoamine oxidase specific activity to approximately 140% of control. Carboxylesterase and formyltetrahydrofolate synthetase activities were not affected by Li+ either in vivo or in vitro.     

Affinity chromatography of monoamine oxidase

Summary A method is described for the purification of pig liver monoamine oxidase by affinity chromatography, using a colum with covalently bound pargyline.Acknowledgment. The authors wish to thank the University Research Council for financial support.     

Distribution of type A and B monoamine oxidase activities in the central nervous system of rat and chick

Summary The distribution of type A and B monoamine oxidase (MAO) activities in the central nervous system (CNS) of rat and chick was investigated using 5-hydroxytryptamine and -phenylethylamine as specific substrates. The distribution of type A MAO was similar to that of type B MAO in rat CNS, but quite different in chick CNS. This may be ascribed to the difference in animal species. The major part of MAO activity in the spinal cord was found to be type A.     

Effect of some monoamine oxidase inhibitors on deamination of biogenic monoamines by rat liver mitochondrial monoamine oxidase

N--N- MAO , , .     

Occurrence of mitochondrial monoamine oxidase in human semen

Summary Mitochondrial monoamine oxidase (MAO) was found in human semen, showing its K_m and V_max values of 91.7 M and 290 pmoles/mg of protein/60 min, respectively, with kynuramine as substrate. A major part of the activity was due to type A MAO.     

Multiple forms of monoamine oxidase in developing Xenopus

Zusammenfassung Das Isoenzymmuster der Monoaminoxidase verändert sich während der frühen Entwicklung der Larven vonXenopus laevis. Die Anzahl elektrophoretischer Banden verkleinert sich während der Entwicklung von vier auf eine.

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The author was supported by a grant from the Cleveland State University Faculty Research Committee. The author would like to express his thanks toJohn Y. Pun the president of Bionix (El Cerrito, California) for the use of the apparatus.     

An anticonvulsant effect of monoamine oxidase inhibitors

Zusammenfassung Inhibitoren der Monoaminoxydase haben eine antikonvulsive Wirkung, die mit einer Erhöhung des Serotonin-und Noradrenalingehaltes im Gehirn verbunden ist. Da anderseits Reserpin durch Freisetzung zu einer Verminderung dieser Amine im Gehirn fürhrt und die Krämpfe verstärkt, ist es wahrscheinlich, dass gewisse physiologisch aktive Amine bei der Entstehung experimenteller Konvulsionen eine entscheidende Rolle spielen. Die Resultate stützen die Annahme, dass gewisse Formen von Epilepsie auf eine lokale Störung im Stoffwechsel der Gehirnamine zurückzuführen sind.

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Fellow, Life Insurance Medical Research Fund.     

Liver monoamine oxidase in normal and regeneratingDiemictylus viridescens

Résumé L'oxydase monoamine se trouve sous une forme active dans le foie d'un urodèle adulte capable d'activité normale et régénératrice. Au cours des deux premières heures qui suivent l'amputation d'un membre antérieur, on peut noter une augmentation appréciable de l'activité de l'oxydase monoamine. Cette augmentation indique que la tension physiologique produite par l'amputation rend actifs dans le foie les précurseurs de l'oxydase monoamine qui peuvent, à leur tour, stimuler un métabolisme plus rapide et augmenter la quantité des catécholamines qui circulent.     

Occurrence of mitochondrial monoamine oxidase in human semen.

Mitochondrial monoamine oxidase (MAO) was found in human semen, showing its Km and Vmax values of 91.7 microM and 290 pmoles/mg of protein/60 min, respectively, with kynuramine as substrate. A major part of the activity was due to type A MAO.