26746
Cholesterol Oxidase from Nocardia erythropolis
in 1 M ammonium sulfate solution, pH 6, solution (slightly hazy), ≥15 U/mL
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About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-842-1
MDL number:
Concentration:
≥15 U/mL
form
solution (slightly hazy)
quality
in 1 M ammonium sulfate solution, pH 6
concentration
≥15 U/mL
color
pale yellow
storage temp.
2-8°C
Other Notes
1 U corresponds to the amount of enzyme which converts 1 μmol cholesterol to 4-cholesten-3-one per minute at pH 7.5 and 25 °C
Conversion of cholesterol to 4-cholesten-3-one; Isomerization of cholest-5-en-3-one to cholest-4-en-3-one; Properties and applications, minireview; Review in clinical biochemistry: The quantitative analysis of cholesterol.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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The mechanism of the isomerization of Cholest-5-en-3-one to cholest-4-en-3-one by cholesterol oxidase [proceedings].
A G Smith et al.
Biochemical Society transactions, 5(4), 1088-1090 (1977-01-01)
Cholesterol oxidases: properties and applications.
A G Smith et al.
Journal of steroid biochemistry, 7(9), 705-713 (1976-09-01)
A G Smith et al.
The Biochemical journal, 167(1), 121-129 (1977-10-01)
1. 5-Cholesten-3-one was shown to be an intermediate in the conversion of cholesterol into 4-cholesten-3-one by Nocardia cholesterol oxidase. 2. The absence of a C-17 side chain from 5-androstene-3,17-dione slightly increased the Vmax. of the isomerase activity relative to 5-cholesten-3-one
Analytical reviews in clinical biochemistry: the quantitative analysis of cholesterol.
W Richmond
Annals of clinical biochemistry, 29 ( Pt 6), 577-597 (1992-11-01)
Vandana Praveen et al.
Applied biochemistry and biotechnology, 165(5-6), 1414-1426 (2011-09-13)
An extracellular cholesterol oxidase (cho) enzyme was isolated from the Streptomyces parvus, a new source and purified 18-fold by ion exchange and gel filtration chromatography. Specific activity of the purified enzyme was found to be 20 U/mg with a 55
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