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Activity staining of plasma amine oxidase after polyacrylamide gel electrophoresis and its application to natural inhibitor screening
Author(s) -
Lee MeiHsien,
Chuang MaoTe,
Hou WenChi
Publication year - 2002
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(200208)23:15<2369::aid-elps2369>3.0.co;2-z
Subject(s) - amine oxidase , chemistry , hydrogen peroxide , chromatography , polyacrylamide gel electrophoresis , peroxidase , benzylamine , amine gas treating , biochemistry , enzyme , organic chemistry
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.