Identification and purification of a novel G protein from neutrophils

Burton F. Dickey, Hae Yung Pyun, Kim C. Williamson, Javier Navarro

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


A novel G protein which appears to couple chemotactic peptide receptors to a polyphosphoinositide phospholipase C has been purified from rabbit neutrophils. Neutrophil membranes were solubilized with sodium cholate and fractionated by successive anion exchange, gel filtration and hydrophobic chromatography. Guanosine-5′-(3-O-thio)triphosphate binding activity was purified 170-fold from the soluble extract. The α-subunit of the purified G protein was identified by pertussis toxin-catalyzed ADP-ribosylation, and found to have an Mr of 40 000. The β-subunit (Mr 36 000) comigrated on SDS-polyacrylamide gel electrophoresis with the β-subunits of bovine brain Gi and Go. The neutrophil pertussis toxin substrate is highly unstable in cholate solution unless 30% ethylene glycol is added. Structural and functional analysis of this novel G protein will advance our understanding of the molecular mechanisms of coupling of receptors to phospholipase C.

Original languageEnglish (US)
Pages (from-to)289-292
Number of pages4
JournalFEBS Letters
Issue number2
StatePublished - Jul 27 1987
Externally publishedYes


  • (Rabbit neutrophil)
  • Guanine nucleotide-binding protein
  • Phospholipase C
  • fMet-Leu-Phe receptor

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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