Abstract
The cholesterol oxidase produced by Rhodococcus equi was purified from the culture broth by procedures including DEAE-Sephadex A-50 and batchwise treatment utilizing the affinity to cholesterol. The purified enzyme was detected as a single band in SDS-PAGE (molecular weight 56000) but in an aggregated form in the electrophoretic patterns on a linear gradient polyacrylamide gel in the presence of Triton X-100. The properties of the purified enzyme were also examined in terms of amino acid composition, isoelectric point, K m value, stability of enzyme activity, metal inhibition, and sensitivity to various modification agents
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