Dialdehyde-GDP blocks activity of cytosolic components of neutrophil NADPH oxidase

Eti Klinger*, Irit Aviram

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Superoxide production by neutrophil NADPH oxidase activated in a cell-free system consisting of plasma membranes, cytosol and arachidonate is enhanced by nonhydrolyzable analogs of GTP and reduced by GDP. To characterize the interaction of guanine nucleotides with the system, dialdehyde analogs of GTP and GDP (oGTP and oGDP) were employed. oGDP or oGTP caused an irreversible and dose dependent inactivation of NADPH oxidase-supporting cytosolic activity. Cytosol was fractionated on S and Q Sepharose ion exchange columns into three fractions, combinations of which synergistically supported activation of NADPH oxidase. Two fractions shown by immunoblotting to contain the oxidase-linked p47 and p67 proteins were inactivated by oGDP. Labeling with [α-32P]-oGTP lead to incorporation of the label into several proteins.

Original languageEnglish
Pages (from-to)504-510
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - 31 May 1991


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