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Clinical Chemistry 19: 1350-1356, 1973;
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Clinical Chemistry, Vol 19, 1350-1356, Copyright © 1973 by the American Association for Clinical Chemistry

Preparation and Properties of a Cholesterol Oxidase from Nocardia sp. and Its Application to the Enzymatic Assay of Total Cholesterol in Serum

W. Richmond 1

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 Dgr4-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 Dgr4- or Dgr5-3beta-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.


Key Words: Dgr4- and Dgr5-3beta-hydroxycholestanes • enzyme kinetics • one-enzyme assay • H2O2 measurement • thin-layer chromatography • Dgr4-cholestenone • ion-exchange chromatography • cellular disruption • ultraviolet spectrophotometry

Submitted on August 7, 1973




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Copyright © 1973 by the American Association for Clinical Chemistry.