Doussiere J, Vignais P V
Département de Biologie Moléculaire et Structurale, Centre d'Etudes Nucléaires, Grenoble, France.
Biochem Biophys Res Commun. 1991 Feb 28;175(1):143-51. doi: 10.1016/s0006-291x(05)81212-4.
The conditions of inhibition of neutrophil O2-. generating oxidase by iodonium biphenyl (IBP) were studied. In a cell free system of oxidase activation consisting of neutrophil membranes and cytosol, GTP-gamma-S, Mg2+ and arachidonic acid, the inhibitory effect of IBP depended on the redox conditions of the medium. Inhibition was observed when the medium was supplemented with dithionite or NADPH. When the cell free system was incubated with IBP in the absence of reducing agents, full oxidase activity was recovered after removal of free IBP by gel filtration. Bovine neutrophil membranes, but not cytosol, contained component(s) sensitive to IBP. Upon treatment of neutrophil membranes by IBP followed by reduction, the spectrum of reduced cytochrome b558 was modified, suggesting that cytochrome b558 is a target site for IBP.