Semicarbazide-sensitive amine oxidase inhibitory and hydroxyl radical scavenging activities of aspartic acid β-hydroxamate and glutamic acid γ-monohydroxamate

Yuh Hwa Liu, Yin Shiou Lin, Tai Lin Lee, Wen Chi Hou

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1 Citation (Scopus)

Abstract

It was reported that semicarbazide-sensitive amine oxidase (SSAO) in plasma was elevated in diabetes mellitus and heart failure. SSAO catalyzed the oxidative deamination of various amines to produce hydrogen peroxide which is one possible source of oxidative stresses. In this research, two amino acid hydroxamates, namely aspartic acid β-hydroxamate (AAH) and glutamic acid γ-monohydroxamate (GAH), showed dose-dependently inhibitory against SSAO from bovine plasma. The IC50 of AAH and GAH was 0.7 mM and 0.023 mM, respectively, in the comparisons with 0.035 mM of semicarbazide (positive controls). The AAH showed mixed noncompetitive inhibition against bovine SSAO in the respect to benzylamine (substrate) and benzylamine-SSAO (substrate-enzyme complex). It was found that the V'max value was reduced and K'm value was increased in the presence of AAH (0.4 mM). Using electron spin resonance to investigate the hydroxyl radical scavenging activities, AAH and GAH showed effectively scavenging activities and IC50 was 0.66 mM and 1.21 mM, respectively.

Original languageEnglish
Pages (from-to)301-306
Number of pages6
JournalBotanical Studies
Volume53
Issue number3
Publication statusPublished - Jul 2012

Keywords

  • Aspartic acid β-hydroxamate (AAH)
  • Electron spin resonance
  • Glutamic acid γ-monohydroxamate (GAH)
  • Hydroxyl radical
  • Semicarbazide-sensitive amine oxidase (SSAO)

ASJC Scopus subject areas

  • Plant Science

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