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Abstract
A purification scheme is described for oxalate oxidase from barley roots. This procedure involves gel filtration on Bio-Gel A 0.5 m and affinity chromatography using oxalate, immobilized on Affi-Gel 10, as a ligand.
The purified enzyme was homogeneous on SDS-gel electrophoresis, thin-layer electrophoresis and high-performance liquid chromatography (HPLC). The molecular weight of the enzyme was 150.000 by SDS-gel electrophoresis and the specific activity was 1.9 U/mg protein.