Estimation of FAD-monooxygenase in microsomal preparations
โ Scribed by Joy Cavagnaro; Elmer J. Rauckman; Gerald M. Rosen
- Publisher
- Elsevier Science
- Year
- 1981
- Tongue
- English
- Weight
- 658 KB
- Volume
- 118
- Category
- Article
- ISSN
- 0003-2697
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โฆ Synopsis
The determination of the mixed function flavin-containing monooxygenase of liver by NADPH oxidation or oxygen uptake is complicated by a significant endogenous rate in the absence of specific substrate. We have defined optimal conditions for measuring this enzyme activity in hepatic microsomal preparations using NADPH oxidation. We have also found that if substrate stimulated minus endogenous NADPH oxidation rates are measured, this enzyme will be underestimated. Data are also presented which suggest that this endogenous rate can be at least partly accounted for by the presence of an endogenous substrate.
๐ SIMILAR VOLUMES
Both the maximum we.Locity and the Michae.U canotati od Xhe oxy,qena.tion od N,N-dimeXhyfaniLLne with the pig k!iveh nichodomal FAV-contain&y monooxggenane (EC J.14.13.b) to N,N-dimtihyLanXine N-oxide appewt 1.7 Qoldn yteaakt in aqueoti bu6de.4 ooLution 06 pff 7.4 than thobe i.n deutetium oxide budd
The activity of flavin-containing monooxygenases in microsomes and whole homogenates is readily estimated by following the thiourea-dependent oxidation of thiocholine. NADPH- and oxygen-dependent flavin-containing monooxygenases catalyze the oxidation of thiourea to formamidine sulfenic acid, which