The activity of one soluble component of the cell-free NADPH:O sub(2) oxidoreductase of human neutrophils depends on guanosine 5'-O-(3-thio)triphosphate

Neutrophil NADPH:O sub(2) oxidoreductase activity, essential in the killing of bacteria by neutrophils, can be elicited in a cell-free system that requires plasma membranes, cytosol and sodium dodecyl sulfate. In addition, GTP or its nonhydrolyzable analog guanosine 5'-3-O-(thio)triphosphate (G...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1990-01, Vol.265 (26), p.15782-15787
Main Authors: olscher, BGJM, Denis, S W, Verhoeven, A J, Roos, D
Format: Article
Language:English
Subjects:
guanosine 5'-O-(3-thio)triphosphate
leukocytes (neutrophilic)
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Neutrophil NADPH:O sub(2) oxidoreductase activity, essential in the killing of bacteria by neutrophils, can be elicited in a cell-free system that requires plasma membranes, cytosol and sodium dodecyl sulfate. In addition, GTP or its nonhydrolyzable analog guanosine 5'-3-O-(thio)triphosphate (GTP gamma S) enhances NADPH oxidase activity. We investigated the mechanism of this effect of GTP- gamma S in the cell-free system. Cytosol from human neutrophils was separated in three different soluble oxidase components (SOC I, SOC II, and SOC III). Previously we reported that the cytosol contains two components which act synergistically. We now report that one component (previously labeled SOC II) contains two different components that can be separated by ion exchange chromatography.
ISSN:0021-9258