Purification and Properties of Amine Oxidase from Epicotyls of Pisum sativum | Zendy

Roy E. McGowan | Zendy; Robert Muir | Zendy

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Purification and Properties of Amine Oxidase from Epicotyls of Pisum sativum

Author(s) -

Roy E. McGowan,

Robert Muir

Publication year - 1971

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.47.5.644

Subject(s) - pisum , sativum , reagent , amine oxidase , enzyme , biochemistry , centrifugation , chemistry , dithiothreitol , chelation , hydroxylamine , amine gas treating , chromatography , etiolation , biology , botany , organic chemistry

A procedure has been developed for the purification of amine oxidase (E.C. 1.4.3.4) from etiolated pea epicotyls (Pisum sativum cv. Little Marvel). The enzyme is sensitive to copper chelating reagents and carbonyl reagents, but is not inhibited by sulfhydryl reagents. The purified enzyme has a molecular weight of 1.85 x 10(5), as determined by sedimentation equilibrium centrifugation, and has been shown to be specifically stimulated by phosphate.

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