The tryptic and chymotryptic fragments of the β-subunit of guanine nucleotide binding proteins in brain are identical to those of retinal transducin

Mark Pines, Peter Gierschik, Allen Spiegel

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

The 35-kDa β-subunit of transducin purified from rod outer segment membranes is cleaved into 2 major fragments by trypsin, and 7 major fragments by chymotrypsin. Identical fragments are visualized by immunoblotting with transducin-β specific antisera after proteolysis of rod outer segment membranes, purified brain guanine nucleotide binding proteins, and brain membranes. The results indicate that the β-subunits of transducin and of brain guanine nucleotide binding proteins are not only similar structurally, but are also similarly oriented in membranes with respect to accessibility to proteolytic enzymes.

Original languageEnglish (US)
Pages (from-to)355-359
Number of pages5
JournalFEBS Letters
Volume182
Issue number2
DOIs
StatePublished - Mar 25 1985
Externally publishedYes

Keywords

  • Adenylate cyclase
  • Guanine nucleotide binding protein
  • Photoreceptor
  • Transmembrane signalling

ASJC Scopus subject areas

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

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