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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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Mechanismen der B-T-Zell-Kooperationd enzyme is reoxidized slowly by oxygen, but in the presence of amines, the rate of reoxidation is markedly enhanced. The extent of enhancement depends on the amine substrate, kynuramine enhancing the rate 125-fold, but 5-hydroxytryptamine only 6-fold. Here we describe the properties of human liver
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https://doi.org/10.1007/978-3-642-68711-2each 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 specifi
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https://doi.org/10.1007/978-3-642-68711-2d biphasic inhibition curves. The position of the plateaus obtained with mitochondria from four animals, indicated that the B form of monoamine oxidase accounted for 30% to 70% of the tyramine deaminating activity. Benzylamine deamination was selectively inhibited by (-)-deprenyl. However, benzylami
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https://doi.org/10.1007/978-3-7091-7792-1 later, Blaschko et al. (1957a,b) established that epinephrine, norepinephrine and dopamine were also substrates for this enzyme. Zeller (1938) distinguished monoamine oxidase as different from several other amine oxidases, such as diamine oxidase. Although it was generally assumed that catecholamin
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https://doi.org/10.1007/978-3-7091-7792-1concentrations (5-160 μM kynuramine) in the presence or absence of 200 mM ETOH were performed with platelets of alcoholics before withdrawal (Alc day 1), one week (Alc day 8) and 3 months (Alc mon 3) after withdrawal as well as in control subjects without and after ETOH intake..In all groups the K.
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