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Purification and characterization of diamine oxidase from clover leaves

Delhaize, E. and Webb, J. (1987) Purification and characterization of diamine oxidase from clover leaves. Phytochemistry, 26 (3). pp. 641-643.

Link to Published Version: http://dx.doi.org/10.1016/S0031-9422(00)84757-3
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Abstract

Diamine oxidase (DAO, EC 1.4.3.6) was purified 135-fold from leaves of subterranean clover (Trifolium subterraneum L. cv Seaton Park) and three isoenzymes were identified. The native enzyme has an M of ca 150 000 and comprises two subunits both having an M, of 80 000. Clover DAO has a broad specificity range and is inhibited by copper ligands and reagents reactive towards carbonyl groups. Copper is essential for enzyme activity with the apoenzyme being reactivated specifically by copper. The enzyme has a broad pH optimum from pH 7-8 and an activation energy of 47 kJ/mol with 1,4-diaminobutane as substrate.

Publication Type: Journal Article
Murdoch Affiliation: School of Mathematical and Physical Sciences
Publisher: Elsevier BV
Copyright: © 1987 Published by Elsevier Ltd.
URI: http://researchrepository.murdoch.edu.au/id/eprint/20626
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