Purification and characterization of oxalate oxidase from wheat seedlings

• Autorzy: Hu Y. , Guo Z.
• Języki publikacji: EN

Abstrakty

EN

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.

• Wydawca: -
• Czasopismo: Acta Physiologiae Plantarum
• Rocznik: 2009
• Tom: 31
• Numer: 2
• Opis fizyczny: p.229-235,fig.,ref.

Twórcy

autor

Hu Y.

• College of Life Science, South China Agricultural University, 510642 Guangzhou, China

autor

Guo Z.

• College of Life Science, South China Agricultural University, 510642 Guangzhou, China

Bibliografia

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