Purification and characterization of the α-bungarotoxin binding protein from rat brain

George Kemp, Linda Bentley, Mark G. McNamee, Barbara J. Morley

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

The α-bungarotoxin (BGT) binding protein from rat brain has been purified and its polypeptide chain composition has been examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Polypeptide chains with Mrs of 55,000, 53,500 and 49,000 have been identified as constituents of the protein. The affinity ligand [3H]maleimidobenzyl trimethylammonium bromide ([3H]MBTA), used to identify the ligand binding site on neuromuscular junction acetylcholine receptors (NMJ AChRs), binds to the 55,000 dalton polypeptide chain. Using a technique where ligands are bound to the protein while the protein is immobilized on α-cobratoxin-Sepharose 4B, it was established that the brain BGT binding protein, like NMJ AChRs, possesses two binding sites for BGT. These experiments reinforce previous evidence that the brain BGT binding protein is closely related but not identical to NMJ AChRs.

Original languageEnglish (US)
Pages (from-to)274-283
Number of pages10
JournalBrain Research
Volume347
Issue number2
DOIs
StatePublished - Nov 18 1985

    Fingerprint

Keywords

  • purification
  • α-bungarotoxin binding protein

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Clinical Neurology
  • Developmental Biology

Cite this