Antibodies against a retinal guanine nucleotide-binding protein cross-react with a single plasma membrane protein in non-retinal tissues

Peter Gierschik, Cyrena Simons, Charles Woodard, Robert Somers, Allen Spiegel

Research output: Contribution to journalArticle

33 Scopus citations


Antisera (AS/1-AS/6) to purified bovine retinal transducin, a guanine nucleotide-binding protein, were produced in 6 rabbits. Immunoblots showed that the antisera varied in their reactivity with the subunits of transducin; AS/1 reacted strongly with all 3 subunits, while the others reacted with only the β and/or γ subunits. Only AS/1 specifically immunoprecipitated the α subunit radiolabeled with non-covalently bound guanine nucleotides. Immunostaining of plasma membrane proteins from non-retinal tissues with AS-1 revealed a single protein (approx. 35 kDa), most likely representing the β subunit of the guanine nucleotide-binding proteins (Gs and gi associated with adenylate cyclase. Cerebral cortex showed the highest content of this protein. Antisera against transducin provide a highly specific and sensitive probe for quantitation of the β subunit of Gs and Gi.

Original languageEnglish (US)
Pages (from-to)321-325
Number of pages5
JournalFEBS Letters
Issue number2
Publication statusPublished - Jul 9 1984
Externally publishedYes



  • Adenylate cyclase
  • Guanine nucleotide-binding protein
  • Retina
  • Rod outer segment membrane

ASJC Scopus subject areas

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

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