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.     

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.     

Monoacylcadaverines as substrates for both monoamine oxidase and diamine oxidase; low rates of activity

Summary Monoacetylcadaverine and monopropionylcadaverine were found to be substrates for both rat liver monoamine oxidase and hog kidney diamine oxidase, but all the K_m-values for the oxidases were very high. The amines were common substrates for type A and type B monoamine oxidase.     

Platelet monoamine oxidase B: Use and misuse

The human platelet in addition to having serotonin (5-HT) receptors, uptake carriers (receptor) and transmitter storage vesicles, primarily possesses mitochondrial monoamine oxidase (MAO) type B. Similar to the major form of MAO in the human brain, this enzyme actively oxidizes A-B and B substrates (tyramine, dopamine, phenylethylamine) as well as the novel secondary amine anticonvulsant, milacemide and dopaminergic neurotoxin, MPTP. 5-HT oxidation is hardly affected by the platelet enzyme and MAO inhibitors have no net effect on its accumulation. MAO-B is selectively inhibited by 1-deprenyl and thus the platelet enzyme may be useful to monitor the anti-Parkinson activity of such drugs, as related to their ability to inhibit brain MAO-B. The oxidation of the anticonvulsant, milacemide, to glycine in vitro and in vivo by MAO-B, may herald new prospects for the development of inert prodrugs capable of being metabolized to neuroactive substances by MAO-B. The plasma levels of their metabolites may be an index of MAO-B activity found in the platelet and brain.     

Platelet monoamine oxidase B: use and misuse

The human platelet in addition to having serotonin (5-HT) receptors, uptake carriers (receptor) and transmitter storage vesicles, primarily possesses mitochondrial monoamine oxidase (MAO) type B. Similar to the major form of MAO in the human brain, this enzyme actively oxidizes A-B and B substrates (tyramine, dopamine, phenylethylamine) as well as the novel secondary amine anticonvulsant, milacemide and dopaminergic neurotoxin, MPTP. 5-HT oxidation is hardly affected by the platelet enzyme and MAO inhibitors have no net effect on its accumulation. MAO-B is selectively inhibited by 1-deprenyl and thus the platelet enzyme may be useful to monitor the anti-Parkinson activity of such drugs, as related to their ability to inhibit brain MAO-B. The oxidation of the anticonvulsant, milacemide, to glycine in vitro and in vivo by MAO-B, may herald new prospects for the development of inert prodrugs capable of being metabolized to neuroactive substances by MAO-B. The plasma levels of their metabolites may be an index of MAO-B activity found in the platelet and brain.     

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.     

Identification of type A monoamine oxidase in mouse and rabbit liver mitochondria

Summary Type A monoamine oxidase was identified in liver mitochondria of mouse and rabbit. 5-Hydroxytryptamine was a common substrate for type A and type B monoamine oxidase in these enzyme preparations where its concentration was 1.0 mM.     

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.     

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.     

Multiplicity of monoamine oxidase in chick brain

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

A new peripheral monoamine oxidase inhibitor: 2,9-dimethyl-β-carbolinium iodide

Resumen Yoduro de 2, 9-dimetilo-carbolinio (DMCI) y no sus metabolitos inhibió la enzyma monoamino oxidasa y elevó¹⁴C-serotonia en el corazón e higado, pero no en el cerebro de ratas.

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This work is taken in part from the M. S. thesis presented byP. M. Gardner to the University of Texas Graduate School of Biomedical Sciences at Houston, 1971.     

Histochemical studies of monoamine oxidase during axonal reaction

Zusammenfassung Es werden Veränderungen der MAO-Aktivität im Rückenmark oder in der Medulla oblongata von Ratten beschrieben, die durch die Sektion des N. ischiadicus oder des N. hypoglossus verursacht wurden.     

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.     

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.