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  • Title: Inhibition of rat aorta semicarbazide-sensitive amine oxidase by 2-phenyl-3-haloallylamines and related compounds.
    Author: Lyles GA, Marshall CM, McDonald IA, Bey P, Palfreyman MG.
    Journal: Biochem Pharmacol; 1987 Sep 01; 36(17):2847-53. PubMed ID: 3632710.
    Abstract:
    The inhibition of semicarbazide-sensitive amine oxidase (SSAO) in rat aorta homogenates by some 2-phenyl-3-haloallylamines has been studied. Derivatives containing a fluorine atom were approximately three times more potent than the corresponding 3-chloroallylamines. These halogen-containing compounds were irreversible inhibitors of SSAO after preincubation with aorta homogenates; kinetic evidence for an initial competitive, reversible interaction (Ki around 0.4-0.6 microM) was found with two compounds (MDL 72145 and 72274). A similar Ki (approx. 0.7 microM) was obtained with 2-phenylallylamine (MDL 72200). However, this compound which lacks a halogen atom was a reversible inhibitor, even after preincubation. The use of a spectrophotometric assay to measure H2O2 production from amine metabolism demonstrated that MDL 72200 was a substrate (Km = 1.4 microM) for SSAO, with a Vmax approximately five times smaller than that of benzylamine (Km = 8.1 microM). Of particular interest in this study is the finding that (E)-2-phenyl-3-chloroallylamine (MDL 72274) is highly selective as an inhibitor of SSAO, compared with MAO-A or B activities, and may be a useful compound for investigating the importance of SSAO in animal tissues.
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