Purification, characterization, and crystallization of monoamine oxidase from escherichia coli k-12

Jung Hyeob Roh, Hideyuki Suzuki, Hiroyuki Azakami, Mitsuo Yamashita, Yoshikatsu Murooka, Hidehiko Kumagai

研究成果: Article査読

39 被引用数 (Scopus)

抄録

The gene for monoamine oxidase (MAO) was cloned from an Escherichia coli genomic library and MAO was overproduced in the periplasmic space. The enzyme was purified to homogeneity by preparation of a periplasmic fraction, followed by ammonium sulfate fractionation and DEAE-cellulose column chromatography. Crystals were obtained by the hanging drop method using sodium citrate as a precipitant. The enzyme was found to be a dimer of identical subunits with a molecular weight of 80,000, and showed the highest activity at pH 7.5 and 45°C. The enzyme was inhibited by a MAO specific inhibitor, hydroxylamine, hydrazine, phenelzine, isoniazid, and tranycypromine. The enzyme oxidized tyramine, phenethylamine, and tryptamine at higher rates, but not oxidized diamine and polyamines such as putrecine and spermine. The antibody against E. coli MAO cross-reacted with purified MAO A from Klebsiella aerogenes.

本文言語English
ページ(範囲)1652-1656
ページ数5
ジャーナルBioscience, Biotechnology and Biochemistry
58
9
DOI
出版ステータスPublished - 1994 1
外部発表はい

ASJC Scopus subject areas

  • バイオテクノロジー
  • 分析化学
  • 生化学
  • 応用微生物学とバイオテクノロジー
  • 分子生物学
  • 有機化学

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