Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/11104
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dc.contributor.authorKumar, Rajender-
dc.contributor.authorHooda, Vinita-
dc.contributor.authorPundir, C S-
dc.date.accessioned2011-02-25T04:17:17Z-
dc.date.available2011-02-25T04:17:17Z-
dc.date.issued2011-02-
dc.identifier.issn0975-0959 (Online); 0301-1208 (Print)-
dc.identifier.urihttp://hdl.handle.net/123456789/11104-
dc.description42-46en_US
dc.description.abstractAn oxalate oxidase was purified to apparent homogeneity from the leaves of 10-days old seedlings of forage Sorghum (Sorghum vulgare var. KH-105). The enzyme had a Mr of 124 kDa with two identical subunits, an optimum pH of 4.5, optimum temperature of 37°C and activation energy (Ea) of 2.0338 Kcal/mol. The rate of reaction was linear up to 7 min. Km value for oxalate was 0.22 mM. The enzyme was stimulated by Cu2+ and inhibited by EDTA, NaCN, diethyldithiocarbamate, na2SO4, but unaffected by NaCl at 0.1 mM concentration. Although the enzyme was stimulated by flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), UV and visible spectra of the enzyme did not match with that of a flavoprotein. The positive reaction of the enzyme with orcinol-H2SO4 reagent indicated its glycoprotein nature. The superiority of the purified enzyme over earlier reported oxalate oxidases for determination of urinary oxalate has been demonstrated.en_US
dc.language.isoen_USen_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rights CC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJBB Vol.48(1) [February 2011]en_US
dc.subjectOxalateen_US
dc.subjectSorghum vulgareen_US
dc.subjectOxalate oxidaseen_US
dc.subjectForage Sorghumen_US
dc.subjectPurificationen_US
dc.subjectGlycoproteinen_US
dc.titlePurification and partial characterization of oxalate oxidase from leaves of forage Sorghum (Sorghum vulgare var. KH-105) seedlingsen_US
dc.typeArticleen_US
Appears in Collections:IJBB Vol.48(1) [February 2011]

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