Summary
A relatively simple method has been described for the rapid purification of D-amino acid oxidase from Trigonopsis variabilis by hydrophobic chromatography on Phenyl-Sepharose CL-4B and negative adsorption on DEAE-cellulose. The purified enzyme had a specific activity of 22–24 units at 25°C and exhibited three bands on enzymatic staining.
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Deshpande, A., Sankaran, K., D'Souza, S.F. et al. A rapid method for the purification of D-amino acid oxidase of Trigonopsis variabilis by hydrophobic chromatography. Biotechnol Tech 1, 55–58 (1987). https://doi.org/10.1007/BF00156288
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DOI: https://doi.org/10.1007/BF00156288