Record Details

Purification and partial characterization of oxalate oxidase from leaves of forage Sorghum (<i style="">Sorghum vulgare</i> var. KH-105) seedlings

NOPR - NISCAIR Online Periodicals Repository

View Archive Info
 
 
Field Value
 
Title Purification and partial characterization of oxalate oxidase from leaves of forage Sorghum (Sorghum vulgare var. KH-105) seedlings
 
Creator Kumar, Rajender
Hooda, Vinita
Pundir, C S
 
Subject Oxalate
Sorghum vulgare
Oxalate oxidase
Forage Sorghum
Purification
Glycoprotein
 
Description 42-46
An 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.
 
Date 2011-02-25T04:17:17Z
2011-02-25T04:17:17Z
2011-02
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/11104
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.48(1) [February 2011]