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- W2190965485 abstract "Publisher Summary This chapter describes the assay and purification procedures, and some properties of the xanthine oxidase from bovine small intestine. The purification procedure involves first, the preparation of crude extract, alumina Cy gel adsorption and elution, first ammonium sulfate fractionation, hydroxylapatite adsorption and elution, second ammonium sulfate fractionation, and finally Diethylaminoethyl cellulose (DEAE)-cellulose column chromatography and concentration of pooled eluates. The properties of xanthine oxidases and dehydrogenases from various sources are comprehensively reviewed. The spectrophotometric method described is satisfactory for measuring xanthine oxidase activity in crude preparations of bovine small intestine. To ascertain the metalloprotein nature of the enzyme, a revised and improved modification of the original procedure for its purification has been developed, which incorporates various techniques for controlling contamination by extraneous metals. Very good yields of highly purified enzyme are consistently obtained with this procedure. Compounds known to be effective electron acceptors for xanthine oxidase are molecular oxygen and the oxidation-reduction dyes, methylene blue and 2, 6-dichlorophenolindophenol. The purified enzyme oxidizes aerobically both hypoxanthine and xanthine to uric acid with a mole-for-mole stoichiometry, and contains no detectable uricase activity." @default.
- W2190965485 created "2016-06-24" @default.
- W2190965485 creator A5089879317 @default.
- W2190965485 date "1967-01-01" @default.
- W2190965485 modified "2023-09-25" @default.
- W2190965485 title "[1] Xanthine oxidase from bovine small intestine" @default.
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- W2190965485 doi "https://doi.org/10.1016/s0076-6879(67)12005-3" @default.
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