Purification and identification of two pertussis-toxin-sensitive GTP-binding proteins of bovine spleen

Biochem Biophys Res Commun. 1989 Jun 30;161(3):1280-5. doi: 10.1016/0006-291x(89)91381-8.

Abstract

Two alpha subunits of GTP-binding proteins were purified from bovine spleen membranes. Both proteins were ADP-ribosylated by pertussis toxin in the presence of beta gamma subunits. The major protein had a molecular mass of 40 kDa and its immunological reactivity and fragmentation pattern by limited proteolysis were identical with those of the alpha subunit of Gi2. The minor protein had a molecular mass of 41 kDa and its partial amino acid sequences completely matched with those predicted from human and rat Gi3 alpha cDNAs.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Chromatography, Ion Exchange
  • GTP-Binding Proteins / isolation & purification*
  • GTP-Binding Proteins / metabolism
  • Humans
  • Macromolecular Substances
  • Molecular Sequence Data
  • Pertussis Toxin*
  • Sequence Homology, Nucleic Acid
  • Species Specificity
  • Spleen / metabolism*
  • Virulence Factors, Bordetella / pharmacology*

Substances

  • Macromolecular Substances
  • Virulence Factors, Bordetella
  • Pertussis Toxin
  • GTP-Binding Proteins