Activity staining of plasma amine oxidase after polyacrylamide gel electrophoresis and its application to natural inhibiro screening

Mei Hsien Lee, Mao Te Chuang, Wen Chi Hou

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Plasma amine oxidase (plasma AO, EC 1.4.3.6) is a copper-containing AO which converts benzylamine (BZ) to benzaldehyde, generating hydrogen peroxide and ammonia. The peroxidase was used as an ancillary enzyme to couple hydrogen peroxide to 3-amino-9-ethylcarbazole (AEC) to achieve plasma AO activity after electrophoresis on native polyacrylamide gels. It was confirmed that plasma AO is inhibited by semicarbazide but neither by clorgyline nor by deprenyl. We also used plasma AO activity staining for the screening of natural inhibitors. This fast and sensitive method can be used in the process of plasma AO purification, characterization, and inhibitor screening.

Original languageEnglish
Pages (from-to)2369-2372
Number of pages4
JournalElectrophoresis
Volume23
Issue number15
DOIs
Publication statusPublished - Aug 2002

Fingerprint

Electrophoresis
Amines
Polyacrylamide Gel Electrophoresis
Screening
Oxidoreductases
Staining and Labeling
Plasmas
Hydrogen Peroxide
Clorgyline
Selegiline
Native Polyacrylamide Gel Electrophoresis
Ammonia
Peroxidase
Purification
polyacrylamide gels
Copper
Enzymes

Keywords

  • Activity staining
  • Amine oxidase
  • Native polyacrylamide gel electrophoresis
  • Screening

ASJC Scopus subject areas

  • Clinical Biochemistry

Cite this

Activity staining of plasma amine oxidase after polyacrylamide gel electrophoresis and its application to natural inhibiro screening. / Lee, Mei Hsien; Chuang, Mao Te; Hou, Wen Chi.

In: Electrophoresis, Vol. 23, No. 15, 08.2002, p. 2369-2372.

Research output: Contribution to journalArticle

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