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pubmed-article:7824646pubmed:abstractTextPea (Pisum sativum L.) seedling amine oxidase (EC 1.4.3.6) is the first amine oxidase to be crystallized that diffracts to atomic resolution (2.5 A). Extensive modifications of a published purification procedure were necessary to obtain protein that would give diffraction-quality crystals. Here we report the improved purification and also use this high-purity protein to reexamine some fundamental characteristics of pea seedling amine oxidase. The extinction coefficient at 280 nm (epsilon 1%(280)) and the molecular mass of the protein are investigated by a variety of techniques, yielding epsilon 1%(280) = 20 cm-1 and a mass 150 +/- 6 kD. In addition, the stoichiometry of the metal and organic cofactors, Cu(II) and 6-hydroxy dopa (Topa) quinone, respectively, is examined. The ratio of Cu(II):Topa:protein monomer is found to be 1:1:1.lld:pubmed
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pubmed-article:7824646pubmed:articleTitlePurification and characterization of pea seedling amine oxidase for crystallization studies.lld:pubmed
pubmed-article:7824646pubmed:affiliationDepartment of Chemistry and Biochemistry, Montana State University, Bozeman 59717.lld:pubmed
pubmed-article:7824646pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7824646pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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