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.     

Normetanephrine and metanephrine oxidized by both types of monoamine oxidase

Summary Both normetanephrine and metanephrine were found to be oxidized by both types of monoamine oxidase in mouse liver mitochondria. Both K_m and V_max values of type B MAO for both substrates were higher than those of type A MAO, which caused the shift of inhibition curves with clorgyline and deprenyl according to the increase in substrate concentration.     

Normetanephrine and metanephrine oxidized by both types of monoamine oxidase

Both normetanephrine and metanephrine were found to be oxidized by both types of monoamine oxidase in mouse liver mitochondria. Both Km and Vmax values of type B MAO for both substrates were higher than those of type A MAO, which caused the shift of inhibition curves with clorgyline and deprenyl according to the increase in substrate concentration.     

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.     

Oxidation of synephrine by type A and type B monoamine oxidase

Summary Synephrine (SP) was found to be a substrate for monoamine oxidase (MAO) in rat brain mitochondria, showing the K_m and V_max values of 250 M and 32.6 nmoles/mg of protein/30 min respectively. The inhibition studies showed that the SP oxidation was carried out by both type A and type B MAO and a major part of the activity was due to type A MAO.     

Acceleration of the rate limiting step in norepinephrine biosynthesis by potassium

Zusammenfassung Kalium erhöht die Bildung von markiertem Noradrenalin aus markiertem Tyrosin im isolierten Vas deferens. Es wird angenommen, dass dieser Effekt auf eine Steigerung der Tyrosin-Hydroxylase zurückzuführen ist.     

Mineralocorticoid treatment and the adrenalectomy-induced increase in monoamine oxidase activity

Summary Bilateral adrenalectomy in the rat results in an increase in heart monoamine oxidase activity in animals drinking water and in animals drinking 0.9% saline. Daily administration of deoxycorticosterone acetate prevented the increased monoamine oxidase activity in the animals drinking saline but not in those drinking water.Acknowledgment. This work was supported in part by a grant from the American Heart Association — Louisiana, Inc.     

Distribution of monoamine oxidase in hippocampal region of the rat

The distribution and development of type A and type B monoamine oxidase (MAO) activities in the hippocampal region of the rat was investigated with biochemical microdetermination. Type A MAO is absolutely dominant and unevenly distributed in the hippocampus. The development of type A MAO in the hippocampus seems to be delayed and reachs adult levels by the 30th day after birth.     

Distribution of monoamine oxidase in hippocampal region of the rat

Summary The distribution and development of type A and type B monoamine oxidase (MAO) activities in the hippocampal region of the rat was investigated with biochemical microdetermination. Type A MAO is absolutely dominant and unevenly distributed in the hippocampus. The development of type A MAO in the hippocampus seems to be delayed and reachs adult levels by the 30th day after birth.     

Ontogenesis of monoamine oxidase in the thyroid gland of rats

Summary During postnatal development, MAO activity in the thyroid gland of male rats increases until day 16, when adult values are reached.     

Inhibition of monoamine oxidase by 3-amino-2-oxazolidinone and 2-hydroxy-ethylhydrazine

Zusammenfassung Die MAO-hemmende Aktivität von 3-Amino-2-Oxazolidinon und von 2-Hydroxy-Äthylhydrazin wird beschrieben.     

Oxidation of synephrine by type A and type B monoamine oxidase.

Synephrine (SP) was found to be a substrate for monoamine oxidase (MAO) in rat brain mitochondria, showing the Km and Vmax values of 250 microM and 32.6 nmoles/mg of protein/30 min respectively. The inhibition studies showed that the SP oxidation was carried out by both type A and type B MAO and a major part of the activity was due to type A MAO.     

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.     

Increase of pyruvic and lactic acid in rat blood by inhibitors of monoamine oxidase

Zusammenfassung Monoaminoxydase(MAO)-Hemmer verschiedener chemischer Klassen sowie Monoamin-Freisetzer erhöhen den Milch- und Brenztraubensäuregehalt im Rattenblut. Der zeitliche Verlauf dieser Vermehrung verhält sich ähnlich wie die 5-Hydroxytryptamin-Akkumulation bzw. -Freisetzung im Gehirn. Im weiteren verstärkt der MAO-Hemmer Iproniazid den durch 5-Hydroxytryptamin oder Noradrenalin bedingten Anstieg von Milch- und Brenztraubensäure im Blut.     

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.     

Subcellular distribution of tyrosine hydroxylase and monoamine oxidase in the bovine caudate nucleus

Zusammenfassung Die subzelluläre Lokalisation von Tyrosin-Hydroxylase und Monoaminoxydase im Nucleus caudatus des Rindergehirns wurde untersucht. Tyrosin-Hydroxylase fand sich grösstenteils in den Synaptosomen, den Mikrosomen und dem Zytoplasma. Eine bedeutende Aktivität von Monoaminoxydase war in den Mitochondrien vorhanden.