Purification and properties of soybean nodule xanthine dehydrogenase |
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Authors: | Eric W. Triplett Dale G. Blevins Douglas D. Randall |
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Affiliation: | 1. Department of Agronomy, University of Missouri, Columbia, Missouri 65211 USA;1. Department of Biochemistry, University of Missouri, Columbia, Missouri 65211 USA |
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Abstract: | Xanthine dehydrogenase (EC 1.2.1.37), an essential enzyme for ureide metabolism was purified from the cytosol fraction of soybean nodules. The purified xanthine dehydrogenase was shown to be homogeneous by electrophoresis and a pI of 4.7 was determined by isoelectric focusing. The enzyme had a molecular weight of 285,000 and two subunits of molecular weight 141,000 each. The holoenzyme contained 1.7 (±0.7) mol Mo and 8.1 (±2.0) mol Fe/mol enzyme and the enzyme also contained FMN and is thus a molybdoironflavoprotein. Soybean xanthine dehydrogenase is the second enzyme in plants demonstrated to contain Mo and the first xanthine-oxidizing enzyme reported to contain FMN, rather than FAD as the flavin cofactor. |
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Keywords: | To whom correspondence should be addressed. |
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