The NADPH oxidase of guinea pig polymorphonuclear leucocytes |
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| Authors: | Paolo Bellavite Maria C. Serra Anna Davoli Joe V. Bannister Filippo Rossi |
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| Affiliation: | (1) Institute of General Pathology, University of Padova at Verona, 37134 Verona, Italy;(2) Inorganic Chemistry Department, University of Oxford, OX1 3QR Oxford, England |
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| Abstract: | Summary 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 µM for NADPH and 434 µM for NADH indicating that NADPH is the preferential substrate. |
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