The NADPH oxidase of guinea pig polymorphonuclear leucocytes. Properties of the deoxycholate extracted enzyme.

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 Biochem

authors

Bellavite P,Serra MC,Davoli A,Bannister JV,Rossi F

doi

10.1007/BF00230585

subject

Has Abstract

pub_date

1983-01-01 00:00:00

pages

17-25

issue

1

eissn

0300-8177

issn

1573-4919

journal_volume

52

pub_type

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