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Cholesterol oxidase from the culture broth of a Pseudomonas sp. was purified with a yield of more than 70% by a one-step procedure using a column of cholesterylglycine-carboxymethylcellulose; active enzyme was eluted by Triton X-100. The purified enzyme was homogeneous by SDS-PAGE.

One-step purification of cholesterol oxidase from culture broth of a Pseudomonas sp. using a novel affinity chromatography method