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Titlebook: Amine Oxidases and Their Impact on Neurobiology; Proceedings of the 4 Peter Riederer,Moussa B. H. Youdim Conference proceedings 1990 Spring

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Molecular neuroanatomy of MAO-A and MAO-Band abundance of MAO-A and MAO-B in the central nervous system and peripheral organs in the rat. The in vitro approach was also used to map the enzymes in human post-mortem brain. Furthermore, using in situ hybridization histochemistry, locus coeruleus and raphé neurons in the human brain were found
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Turnover of monoamine oxidase B (MAO-B) in pig brain by positron emission tomography using 11C-L-depirreversible ligand, which bind stoichiometrically to the enzyme. A tracer dose of. C-L-deprenyl was injected and PET scans performed to obtain baseline deprenyl binding. A high dose of unlabelled deprenyl was then administered to inhibit the enzyme and tracer doses of . C-L-deprenyl, with subsequen
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Some pharmacological implications of MAO-mediated deamination of branched aliphatic amines: 2-Propylbazide-sensitive amine oxidase. The deaminated product, valproic acid (VPA), was identified by HPLC-fluorometric assessment. Absorption and biotransformation of these compounds and their VPA metabolite into the brain were rapid processes. An investigation was conducted to examine whether these compo
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Ring-substituted analogues of tranylcypromine as monoamine oxidase inhibitorstested for their ability to inhibit, relative to tranylcypromine, monoamine oxidase (MAO) -A and -B in rat brain after administration of low doses (1.2 and 3.7 μmol/kg) of the drugs. One hour after intraperitoneal injection of the lower dose, tranylcypromine was weaker than 4-fluorotranylcypromine a
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Stylbasole analogues of MPTP as monoamine oxidase (MAO) substrates compounds was shown to be catalyzed by both serotonine specifical and benzylamine specifical MAO activities. Markedly high affinity of stylbasoles to B type of MAO was found. Influence of substrate structure on its biotransformation effectiveness is realized by the principle — “better binding-worse
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