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Titlebook: Amine Oxidases: Function and Dysfunction; Proceedings of the 5 K. F. Tipton,M. B. H. Youdim,G. A. Lyles Conference proceedings 1994 Springe

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期刊全稱Amine Oxidases: Function and Dysfunction
期刊簡(jiǎn)稱Proceedings of the 5
影響因子2023K. F. Tipton,M. B. H. Youdim,G. A. Lyles
視頻videohttp://file.papertrans.cn/155/154676/154676.mp4
學(xué)科分類Journal of Neural Transmission. Supplementa
圖書(shū)封面Titlebook: Amine Oxidases: Function and Dysfunction; Proceedings of the 5 K. F. Tipton,M. B. H. Youdim,G. A. Lyles Conference proceedings 1994 Springe
影響因子Monoamine oxidase plays a major role in the pathogenesis of neuropsychiatric disorders including depressive illness, Parkinson′s disease and Alzheimer′s disease. The new generation of selective monoamine oxidase inhibitors, devoid of major side effects, has found a prominent place in the treatment of these diseases. Some of these drugs may have neuroprotective activity with prospects for treating progressive neurodegenerative diseases. The volume presents a collection of research papers on monoamine oxidase and its inhibitors. The topic is treated from the point of view of chemistry, biochemistry, pharmacology, physiology, neurology and psychiatry. The book serves as a quick and comprehensive reference source for obtaining the most up to date information.
Pindex Conference proceedings 1994
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Amine Oxidases: Function and Dysfunction978-3-7091-9324-2Series ISSN 0303-6995
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https://doi.org/10.1007/978-3-7091-7792-1eparations. Kinetic considerations show that the rate of reaction of MAO-A with low concentrations of free pargyline will be very much slower than that of MAO-B. Failure to use adequate reaction times for the concentration of pargyline added can lead to gross underestimation of the quantity of MAO-A present.
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Identification of human monoamine oxidase (MAO) A and B gene promoterseach of which contains two Sp1 elements and lacks a TATA box. The MAO B core promoter region contains two sets of overlapping Spl sites which flank a CACCC element all upstream of a TATA box. The different organization of the MAO A and B promoters may underlie their different cell and tissue specific expression.
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Estimation of monoamine oxidase concentrations in soluble and membrane-bound preparations by inhibiteparations. Kinetic considerations show that the rate of reaction of MAO-A with low concentrations of free pargyline will be very much slower than that of MAO-B. Failure to use adequate reaction times for the concentration of pargyline added can lead to gross underestimation of the quantity of MAO-A present.
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