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.
journal_name
Mol Cell Biochemjournal_title
Molecular and cellular biochemistryauthors
Bellavite P,Serra MC,Davoli A,Bannister JV,Rossi Fdoi
10.1007/BF00230585subject
Has Abstractpub_date
1983-01-01 00:00:00pages
17-25issue
1eissn
0300-8177issn
1573-4919journal_volume
52pub_type
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