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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Immunoaffinity purification of an oxidase-activating cytosolic complex from bovine neutrophils.

An oxidase activating complex from the cytosol of bovine neutrophils was purified by immunoaffinity using a monoclonal antibody specific for the 67 kDa cytosolic factor of oxidase activation ( p67) and assayed for production of superoxide O2- in a cell-free system. The complex comprised not only p67, but also the second cytosolic factor of 47 kDa (p47) in equivalent amounts. The p47-p67 complex showed a good oxidase activating potency when added to neutrophil membranes in the presence of GTP-gamma-S and arachidonic acid. A ras-related small G protein could not be immunodetected in the p47-p67 activating complex, indicating that the GTP required for oxidase activation in the cell free system bound to a protein that was either present in catalytic amounts in the cytosolic complex or present in sufficient amount in the membrane fraction.[1]

References

  1. Immunoaffinity purification of an oxidase-activating cytosolic complex from bovine neutrophils. Jouan, A., Dagher, M.C., Fuchs, A., Foucaud-Gamen, J., Vignais, P.V. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
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