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.     

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.     

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.     

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.     

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.     

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.     

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.     

Differential activation of two monoamine oxidase types by oxygen

Summary The stimulation of rat brain monoamine oxidase activity by oxygen is shown to be type-selective, type B being much more strongly stimulated than type A.Pargyline and clorgyline were gift samples from Abbott Laboratories, USA and May and Baker Ltd, England respectively     

Methoxyphenylethylamines as substrates for type A and type B monoamine oxidase

Summary 4-Methoxyphenylethylamine was found to be a specific substrate for type B monoamine oxidase (MAO) in rat brain mitochondria, whereas 3,4-dimethoxyphenylethylamine was common for both types of MAO. These results suggest that O-methylation in the para-position increases the preference of the substrate for type B MAO, while a methoxy-group in the meta-position contributes to the substance being a type A substrate.     

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.     

Monoamine oxidase inhibition by d-amphetamine in ganglia and nerve endings

Summary The inhibition of monoamine oxidase (MAO) activity by d-amphetamine was measured in homogenates of cat superior cervical ganglion and nictitating membrane, using tyramine (TM) and noradrenaline (NA) as substrates. In both tissues, d-amphetamine was shown to be a competitive inhibitor of the oxidation of TM. The Ki for d-amphetamine, as a MAO inhibitor, was lower in the ganglia than in the peripheral nerve endings.Supported by a Contract from the National Research Council of Argentina (CONICET) (Res. 67/79).     

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.     

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.     

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.     

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.     

Monoamine oxidase activity in rat erythrocytes: Evidence for its localization in reticulocyte mitochondria

Summary During growth of young rats, monoamine oxidase activity in erythrocyte membrane preparations decreases more rapidly than reticulocyte concentrations in the respective blood samples. Since reticulocytes lose their mitochondria prior to the substantia reticulo-filamentosa, the non-linear correlation between monoamine oxidase activity and reticulocyte counts indicates that erythrocyte monoamine oxidase is located in reticulocyte mitochondria.This work was supported by a grant from the Deutsche Forschungsgemeinschaft.     

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.     

Purification and some properties of an amine oxidase from soybean seedlings

Summary An amine oxidase was purified 447-fold from soybean seedlings and some of its properties were investigated. The molecular weight of the enzyme was estimated to be 25,000. It was most active towards putrescine, followed by spermidine and spermine. K_m-values for these substrates were relatively close. The enzyme was strongly inhibited by carbonyl reagents, such as semicarbazide and aminoguanidine.