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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-Kooperationme, but the steady-state parameters for the endogenous amines are the same. Tertiary amines are oxidized at slightly different rates by the two enzymes. The consequences of the branched pathway mechanism with substrate-dependent enhancement of reoxidation for the steady-state levels of the various enzyme species is discussed.
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Kinetic properties of cloned human liver monoamine oxidase Ame, but the steady-state parameters for the endogenous amines are the same. Tertiary amines are oxidized at slightly different rates by the two enzymes. The consequences of the branched pathway mechanism with substrate-dependent enhancement of reoxidation for the steady-state levels of the various enzyme species is discussed.
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Some kinetic properties of guinea pig liver monoamine oxidaseig liver enzyme. Guinea pig liver contains a monoamine oxidase-B which is unusual in that although it exhibits apparently normal sensitivity to selective irreversible inhibitors, it has a low catalytic activity with substrates which the enzyme from rat liver deaminates rapidly.
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Monoamine oxidase (MAO; E.C. 1.4.3.4) characteristics of platelets influenced by in vitro and in viv each group..The V. of Alc day 1 is significantly 25% decreased, of Alc day 8 unchanged and of Alc mon 3 nonsignificantly 19% decreased in comparison with the controls. The increase of the K. in the presence of 200 mM ETOH is significantly 15% reduced in Alc day 1 and 9% in Alc day 8 but unchanged in Alc mon 3 compared with the controls.
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Functional expression of C-terminally truncated human monoamine oxidase type A in ,to other flavoproteins identified a single potential transmembrane hydrophobic peptide at the C-terminus suggesting that this peptide is a membrane anchor and that the remainder of the protein constitutes a soluble domain. Truncation of the C-terminus by 24 amino acids which are inclusive of the put
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