| Literature DB >> 6865930 |
P Bellavite, M C Serra, A Davoli, J V Bannister, F Rossi.
Abstract
NADPH oxidase from stimulated guinea pig granulocytes was extracted with deoxycholate. The solubilized enzyme was stable in 20% glycerol. Solubilized enzyme was free of myeloperoxidase activity. The properties of the deoxycholate solubilized enzyme indicated that it is a high molecular weight complex with a flavoprotein, calmodulin and cytochrome b possibly forming part of the complex. Maximum activity was between pH 7.0 and 7.5. The Km value was 15.8 microM for NADPH and 434 microM for NADH indicating that NADPH is the preferential substrate.Entities:
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Year: 1983 PMID: 6865930 DOI: 10.1007/bf00230585
Source DB: PubMed Journal: Mol Cell Biochem ISSN: 0300-8177 Impact factor: 3.396