Electrophoretic separation of betaA4 peptides (1-40) and (1-42)

Anal Biochem. 1996 May 15;237(1):24-9. doi: 10.1006/abio.1996.0195.


Different sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) systems designed for the separation of peptides were compared for their usefulness in separating synthetic beta-amyloid peptides betaA4 (1-40) and betaA4 (1-42). Clear resolution was achieved by addition of 8 M urea to the separation gel and use of a multiphasic buffer system employing bicine and sulfate as trailing and leading ions, respectively (bicine/Tris/urea gels). Under these conditions, the longer peptide migrated faster than the one ending at amino acid 40. The usefulness of this SDS-PAGE system for the analysis of betaA4-related peptides generated during cellular metabolism was demonstrated by immunoprecipitation and electrophoretic separation of radiolabeled peptides secreted by cells transfected with amyloid precursor protein cDNAs.

MeSH terms

  • Amyloid beta-Peptides / analysis*
  • Animals
  • Cells, Cultured
  • Electrophoresis, Polyacrylamide Gel
  • Peptide Fragments / analysis*
  • Rabbits


  • Amyloid beta-Peptides
  • Peptide Fragments
  • amyloid beta-protein (1-40)