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KMID : 0380219930260020192
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Journal of Biochemistry and Molecular Biology
1993 Volume.26 No. 2 p.192 ~ p.198
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Purification and Properties of Ornithine Decarboxylase from Glycine max Axes
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Dong Chung Kim and Young Dong Cho
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Abstract
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Ornithine decarboxylase (EC 4.1.1.17) was purified to homogeneity from soybeans, Glycine max, axes by chromatographic separations on DEAF-Sephacel, Hydroxyapatite and phenyl-Sepharose with the addition of 15% glycerol. The molecular weight of the enzyme estimated by Sephacryl S-300 gel filtration and SDS-PAGE was 55,000 daltons and monomeric. The optimal pH and temperature were 8.5 and 40℃, respectively, and K_m was 0.135 mM. Carbonyl group and cysteinyl residue seem to be involved in enzyme activity. DFMO was a potent suicide inhibitor while metal ions, agmatine and polyamines were innocuous for the enzymatic activity.
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