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

Article Details

Citation

Copy to clipboard

Tipnis UR, Tao M, Boor PJ

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

Cell Mol Biol (Noisy-le-grand). 1992 Aug-Sep;38(5-6):575-84.

PubMed ID

1483111 [ View in PubMed

]

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.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Phenelzine	Membrane primary amine oxidase	Protein	Humans	Unknown	Inhibitor	Details