Immunoaffinity purification of an oxidase-activating cytosolic complex from bovine neutrophils. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Biochemical and Biophysical Research Communications Année : 1993

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

A. Jouan
  • Fonction : Auteur
Alexandra Fuchs
J. Foucaud-Gamen
  • Fonction : Auteur
P. V. Vignais
  • Fonction : Auteur

Résumé

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.

Domaines

Immunité innée
Fichier non déposé

Dates et versions

hal-00820799 , version 1 (06-05-2013)

Identifiants

  • HAL Id : hal-00820799 , version 1
  • PUBMED : 8280146

Citer

A. Jouan, M. C. Dagher, Alexandra Fuchs, J. Foucaud-Gamen, P. V. Vignais. Immunoaffinity purification of an oxidase-activating cytosolic complex from bovine neutrophils.. Biochemical and Biophysical Research Communications, 1993, 197 (3), pp.1296-302. ⟨hal-00820799⟩

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