Plant Physiol. Drug Metab Dispos
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PLANT PHYSIOLOGY , Vol 106, Issue 3 1205-1211, Copyright © 1994 by American Society of Plant Biologists

METABOLISM AND ENZYMOLOGY

Purification and Characterization of Pea Seedling Amine Oxidase for Crystallization Studies

M. A. McGuirl, C. D. McCahon, K. A. McKeown and D. M. Dooley
Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717

Pea (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 of 150 [plus or minus] 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.


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Copyright © 1994 by the American Society of Plant Biologists