Showing papers on "Monoamine oxidase B published in 1968"
TL;DR: The hypothesis that in the enzyme prepared, the MAO is a binary system of enzymes each of which has a detectably different sensitivity to this particular inhibitor, is put forward and evidence after dialysis supports this hypothesis.
1,557 citations
TL;DR: Several tricyclic compounds of iminodibenzyl or cycloheptadiene structure which do not inhibit MAO are also effective antidepressant drugs, and seem to act by inhibiting the re-uptake inactivation of noradrenaline4–7 and potentiating its effects in the brain.
Abstract: MONOAMINE oxidase (MAO) inhibitors were the first clinically used antidepressant drugs. Several tricyclic compounds of iminodibenzyl or cycloheptadiene structure which do not inhibit MAO are also effective antidepressant drugs (refs. 1–3 and unpublished work of J. M. Davis, G. L. Klerman and J. J. Schildkraut), and seem to act by inhibiting the re-uptake inactivation of noradrenaline4–7 and potentiating its effects in the brain.
103 citations
TL;DR: Compound 51641 thus is a potent inhibitor of MAO in vitro and in vivo and was not reversible by dialysis and was independent of enzyme concentration.
56 citations
TL;DR: Initial rate measurements of the oxidation of tyramine were carried out with purified pig brain mitochondrial monoamine oxidase, and reciprocal plots obtained gave families of parallel lines consistent with a kinetic mechanism in which a ternary complex is not involved.
Abstract: Initial rate measurements of the oxidation of tyramine were carried out with purified pig brain mitochondrial monoamine oxidase. The reciprocal plots obtained when the concentration of either substrate was varied at a series of fixed concentrations of the other gave families of parallel lines consistent with a kinetic mechanism in which a ternary complex is not involved. This mechanism was supported by product inhibition studies and the demonstration of a half-reaction in the absence of oxygen.
51 citations
TL;DR: Some properties of the different bands of MAO activity isolated from human and rat liver mitochondria are reported in this manner.
49 citations
TL;DR: Thyroid monoamine oxidase exhibited a rather high degree of substrate specificity and was not inhibited by carbonyl reagents which suggests that the thyroid enzyme may not contain pyridoxal phosphate.
44 citations
TL;DR: Reserpine activates rat microsomal monoamine oxidase to a greater extent than the mitochondrial enzyme and inhibits aldehyde dehydrogenase, which may account for the previously observed shift of urinary metabolite ratios after its administration.
29 citations
TL;DR: The separation of solubilized liver mitochondrial monoamine oxidases from three species by gel filtration in the presence of detergent reveals at least three different monoamine oxidationases present in rat and rabbit liver and at least two in beef liver.
27 citations
TL;DR: The time-courses of inhibition of the activity of pig brain mitochondrial monoamine oxidase by 2-bromo-2-phenylacetaldehyde toward the substrates tyramine, tryptamine, 5-hydroxytryptamine, adrenaline and m-O-methylnoradrenaline have been found to be the same.
24 citations
22 citations
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TL;DR: Selective inhibition by MAOI of enzymatic deamination of various biogenic monoamines in vivo is possible but the patterns of this selectivity in various tissues could not be predicted on the basis of in vitro experiments with a standard preparation of liver mitochondrial MAO.
TL;DR: It is demonstrated that α-methylated analogues of noradrenaline taken up by adrenergic neurons are slowly released by inhibitors of monoamine oxidase, but this release is inhibited by pretreatment with dopa/5-HTP inhibitors such as 3-hydroxy-benzylhydrazine and seryl-2, 3, 4-trihydroxybenzymethine.
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TL;DR: Measurement of brain catecholamines after monoamine oxidase inhibition shows a faster and greater increase in the adult rat than the in the infant.
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