BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS Pages 430-436 CATALYTIC PROPERTIES OF THE RESOLVED FLAVOPROTEIN AND CYTOCHROME B COMPONENTS OF THE NADPH DEPENDENT 0 -. GENERATING OXIDASE FROM HUMAN NEUTRO
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چکیده
The resolved flavoprotein and cytochrome b55g components of the NADPH dependent 0 -. further f generating oxidase from human neutrophils were the subject of stu y. The resolved flavoprotein, depleted of cytochrome bssg, was reduced by NADPH under anaerobic conditions and reoxidized by oxygen. NADPH dependent 02-. generation by the resolved flavoprotein fraction was not detectable, however it was competent in the transfer of electrons from NADPH to artificial electron acceptors. The resolved cytochrome b559, depleted of flavoprotein, demonstrated no measureable NADPH dependent O2 . generating activity and was not reduced by NADPH under anaerobic conditions. The dithionite reduced form of the resolved cytochrome bssg was rapidly oxidized by oxygen, as was the cytochrome bssg in the intact oxldase.
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