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Indian Journal of Biochemistry and Biophysics (IJBB) >
IJBB Vol.48 [2011] >
IJBB Vol.48(1) [February 2011] >
| Title: | Purification and partial characterization of oxalate oxidase from leaves of forage Sorghum (Sorghum vulgare var. KH-105) seedlings |
| Authors: | Kumar, Rajender
Hooda, Vinita
Pundir, C S |
| Keywords: | Oxalate
Sorghum vulgare
Oxalate oxidase
Forage Sorghum
Purification
Glycoprotein |
| Issue Date: | Feb-2011 |
| Publisher: | NISCAIR-CSIR, India |
| Abstract: | 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. |
| Page(s): | 42-46 |
| CC License: |  CC Attribution-Noncommercial-No Derivative Works 2.5 India |
| ISSN: | 0975-0959 (Online); 0301-1208 (Print) |
| Source: | IJBB Vol.48(1) [February 2011]
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