Large scale preparation and purification of apo-D-aminoacid oxidase for use in novel amplification assays |
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| Authors: | Stuart Harbron Mark Fisher Brian R. Rabin |
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| Affiliation: | (1) London Biotechnology Ltd, Department of Biochemistry and Molecular Biology, University College London, Gower Street, WC1E 6BT London, UK |
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| Abstract: | Summary Dissociation of FAD from D-aminoacid oxidase occurred most rapidly at pH 6.0 in the presence of 1 M KBr. Diafiltration of 0.6 g of enzyme under these conditions yielded apoenzyme containing 1.3% of residual holoenzyme activity, which was subsequently reduced to less than 0.01% by chromatography on Blue Sepharose and ion exchange, giving material containing <1 ppb of contaminating phosphatase and nucleotidase. |
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