Cellular forms of the rat and human ß-amyloid precursor protein (BAPP)

John Anderson, William Wallace, Susan Snyder, Vahram Haroutunian, James L. Roberts, Ivan Lieberburg

Research output: Contribution to journalArticlepeer-review

10 Scopus citations


Using synthetic peptide antisera generated against ß-amyloid precursor protein (BAAP) sequences we demonstrate that the newly synthesized BAPP appears as a 94 kDa peptide in rat brain RNA cell-free translates or polysome runoffs, while from similar human brain material we see two bands at 94 and 120 kDa. Immunoblots reveal likely post-translational modification of BAPP, and possibly an age-dependent, endogenous proteolysis of the protein in rat brain. On human brain immunoblots an unusual post-translational modification or possibly oligomerization of BAPP is seen, particularly in cortical regions.

Original languageEnglish (US)
Pages (from-to)391-398
Number of pages8
JournalBrain Research
Issue number2
StatePublished - Jan 30 1989
Externally publishedYes


  • Alzheimer's disease
  • Cell-free translation
  • Polysome runoff, Messenger ribonucleic acid
  • Processing
  • ß-Amyloid precursor protein

ASJC Scopus subject areas

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


Dive into the research topics of 'Cellular forms of the rat and human ß-amyloid precursor protein (BAPP)'. Together they form a unique fingerprint.

Cite this