Purification and characterization of oxalate oxidase from wheat seedlings

被引：0
|
作者：
Yihong Hu
Zhenfei Guo
机构：
[1] South China Agricultural University,College of Life Science
来源：
Acta Physiologiae Plantarum | 2009年 / 31卷
关键词：
Characterization; Chemical modification; Oxalate oxidase; Protein purification; Wheat;
D O I：
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中图分类号：
学科分类号：
摘要：
Oxalate oxidase (OxO, EC 1.2.3.4.) was purified to homogeneity from wheat (Triticum aestivum) seedlings by sequential thermal treatment, ultrafiltration, Sephadex G-100 gel filtration and affinity chromatography with concanavalin A. The enzyme was purified 66.11-fold with a recovery of 21.97%. It showed a subunit molecular mass of 32.6 kDa on SDS-PAGE and a native molecular mass of 170 kDa on Sephadex G-150 filtration, suggesting that it is a pentamer. The wheat OxO had a maximum activity at pH 3.5. Its Km for oxalate was 0.21 mM. Chemical modification revealed that cysteine, lysine and carboxylate residues were essential for OxO activity, whereas arginine, serine, threonine and tryptophane residues were not essential.
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页码：229 / 235
页数：6
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