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Clinical Chemistry, Vol 19, 1350-1356, Copyright © 1973 by the American Association for Clinical Chemistry
1 Division of Clinical Chemistry, Medical Research
Council, Clinical Research Centre, Harrow, Middlesex, England.
I describe the characterization, extraction, and purification of a cholesterol:oxygen oxidoreductase (EC
1.1.3.6) from Nocardia sp. This enzyme catalyzes
oxidation of cholesterol to 
4-choIestenone, with
production of hydrogen peroxide. It is very stable,
active over a wide pH range, and has a Km of 1.4 x
10-5 mol/ liter. It is highly specific for
4- or 5-3
-hydroxycholestanes, and may be applied to the
assay of serum total cholesterol. In the procedure
presented here, hydrogen peroxide is measured by
reaction with quadrivalent titanium and xylenol orange. This constitutes a one-enzyme assay with stable reagents, which does not require protein precipitation and is not subject to interference from hemoglobin or bilirubin.
4- and 5-3-hydroxycholestanes • enzyme kinetics • one-enzyme assay • H2O2 measurement • thin-layer chromatography • 4-cholestenone • ion-exchange chromatography • cellular disruption • ultraviolet spectrophotometry
Submitted on August 7, 1973
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