Purification and characterization of semicarbazide-sensitive amine oxidase from porcine aorta.

U. R. Tipnis, M. Tao, P. J. Boor

Research output: Contribution to journalArticle

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Abstract

We purified semicarbazide-sensitive amine oxidase (SSAO) from porcine aorta by sequential DEAE-Sephacel, DEAE-Sephadex and Affi-gel-Con A chromatography. The analysis of this protein under denaturing conditions exhibited two protein bands migrating at 110-107 kDa. Under non-denaturing conditions only a single protein band was observed. By isoelectric focusing pI of SSAO was estimated to be 5.5. The apparent Km and Vmax of porcine SSAO for oxidation of benzylamine were 4.5 microM and 200 nmol/hr/mg protein, respectively. Porcine SSAO was inhibited both by semicarbazide and phenelzine while deprenyl or clorgyline were without any effect on enzyme activity. IC50 for inhibition of semicarbazide and phenelzine was 0.015 microM and 1 nmol, respectively.

Original languageEnglish (US)
Pages (from-to)575-584
Number of pages10
JournalCellular and Molecular Biology
Volume38
Issue number5-6
StatePublished - Aug 1992

Fingerprint

Amine Oxidase (Copper-Containing)
Purification
Aorta
Swine
Phenelzine
Proteins
Clorgyline
Enzyme inhibition
Selegiline
DEAE-Dextran
Enzyme activity
Isoelectric Focusing
Chromatography
Inhibitory Concentration 50
Gels
Oxidation
Enzymes
carbamylhydrazine

ASJC Scopus subject areas

  • Cell Biology
  • Clinical Biochemistry
  • Molecular Biology

Cite this

Purification and characterization of semicarbazide-sensitive amine oxidase from porcine aorta. / Tipnis, U. R.; Tao, M.; Boor, P. J.

In: Cellular and Molecular Biology, Vol. 38, No. 5-6, 08.1992, p. 575-584.

Research output: Contribution to journalArticle

Tipnis, U. R. ; Tao, M. ; Boor, P. J. / Purification and characterization of semicarbazide-sensitive amine oxidase from porcine aorta. In: Cellular and Molecular Biology. 1992 ; Vol. 38, No. 5-6. pp. 575-584.
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