Immunoaffinity purification and characterization of diamine oxidase from Cicer |
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Authors: | Riccardo Angelini Filomena Di Lisi Rodolfo Federico |
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Institution: | Department of Plant Biology, ‘La Sapienza’ University of Rome, P. le Aldo Moro 5, 00185 Rome, Italy |
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Abstract: | Antiserum specific for diamine oxidase (DAO;EC 1.4.3.6) from Lens culinaris cross-reacted with DAO from several other members of the Leguminosae when tested by agar double diffusion. Antibodies purified by affinity chromatography were used to make an immunoadsorbent for the one-step purification of DAO from various species of the Leguminosae. This technique has made it possible to purify in one step the already characterized DAO from pea and lentil, and the unknown diamine oxidase from Cicer arietinum. This enzyme was partially characterized; it showed a pH optimum of 7.5 with putrescine as substrate and followed typical Michaelis-Menten kinetics with a Km of 2.4 × 10?4 M. Copper ligands and carbonyl group-directed reagents inhibited the enzyme. |
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Keywords: | Leguminosae diamine oxidase immunoaffinity purification |
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