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dc.contributor.authorQin, W.
dc.contributor.author王勤
dc.contributor.authorChen, QX
dc.contributor.author陈清西
dc.contributor.authorHuang, XH( Biocide Research Center, Fujian Agriculture and Forestry University)
dc.contributor.authorKe, LN
dc.contributor.authorYan, S
dc.contributor.author石艳
dc.contributor.authorJun,W
dc.date.accessioned2011-10-20T10:04:50Z
dc.date.available2011-10-20T10:04:50Z
dc.date.issued2004
dc.identifier.citationBiochemistry (Moscow), Vol. 69, No. 8, 2004, pp. 918 920. Translated from Biokhimiya, Vol. 69, No. 8, 2004, pp. 1129-1132.zh_CN
dc.identifier.issn0006-2979
dc.identifier.urihttp://dx.doi.org/doi:10.1023/B:BIRY.0000040225.33267.26
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10963
dc.description.abstractPolyphenol oxidase (EC 1.14.18.1) was purified from the pupae of blowfly (Sarcophaga bullata) by a procedure involving ammonium sulfate fractionation and chromatography on DEAE-cellulose and Sephadex G-100. Kinetic characteristics of the enzyme were determined using L-DOPA as substrate. The specific activity of the enzyme was 770 U/mg, and the Michaelis constant (Km) was 1.5 +/- 0.1 mM (pH 6.8, 30degreesC). Activity was maximal at 40degreesC, pH 6.5. Chemical modification experiments demonstrated that cysteine and tryptophan residues are essential and arginine residues are not essential to the enzyme function. The enzyme is inhibited by quercetin with an IC50 of 0.20 +/- 0.06 mM. The inhibition is of competitive type, and the inhibition constant was determined to be 88 muM.zh_CN
dc.language.isoenzh_CN
dc.publisherMAIK NAUKA/INTERPERIODICAzh_CN
dc.subjectpolyphenol oxidasezh_CN
dc.subjectblowfly pupaezh_CN
dc.subjectkinetic characterizationzh_CN
dc.subjectchemical modificationzh_CN
dc.titleEnzymatic characterization and functional groups of polyphenol oxidase from the pupae of blowfly (Sarcophaga bullata)zh_CN
dc.typeArticlezh_CN


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