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- W2364453821 abstract "The specific activity of Candida utilis uricase was increased by 20-fold after chromatography twice on DEAE-cellulose 52.SDS-PAGE resolved a single polypeptide of about 33.0 kD.The molecular weight of the native uricase was 134.0 kD by gel filtration through Sephadex G-200.Matrix-assisted laser desorption ionization time-of-flight MS analysis resolved a 67.7 kD polypeptide as the principal component and a 131.4 kD polypeptide of slightly lower abundance,but no single polypeptide was detected,with uricase sample of specific activity 7.0 U/mg protein.The optimum pH for this uricase was approximately 8.8.This uricase was stable at 37oC for 4 h and more than 50% activity was reserved at pH 7.4.The Michaelis-Menten constant was(32.8±3.1) μmol/L(n=10) and the inhibition constant of xanthine was(4.8±0.2) μmol/L(n=3).The activity decreased by 90% after dialysis against distilled water,which was not restored by treatment with NaCl.This uricase was inhibited markedly by 1.0 mmol/L Cu2+ and 1.0 mmol/L Fe3+.These results suggested that molecular engineering to this Candida utilis uricase may benefit its use as a drug to treat diseases associated with hyperuricemia." @default.
- W2364453821 created "2016-06-24" @default.
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- W2364453821 date "2008-01-01" @default.
- W2364453821 modified "2023-09-27" @default.
- W2364453821 title "Purification and Characterization of the Uricase from Candida utilis" @default.
- W2364453821 hasPublicationYear "2008" @default.
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