Inhibition of Aminopeptidase and Acetylcholinesterase by Puromycin and Puromycin Analogs

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


Abstract: Puromycin analogs in which the O‐methyl‐L‐tyrosine moiety was substituted by a number of amino acids were examined as inhibitors of the puromycin‐sensitive rat brain aminopeptidase and bovine erythrocyte acetyl‐cholinesterase. In the case of the aminopeptidase, the structure and stereochemistry of the amino acid substituent were important factors in determining inhibitor effectiveness. In the case of the acetylcholinesterase reaction, the aminonucleoside of puromycin was nearly as effective an inhibitor as puromycin itself, with little effect dependent on the nature or stereochemistry of the amino acid.

Original languageEnglish
Pages (from-to)1594-1596
Number of pages3
JournalJournal of Neurochemistry
Issue number4
StatePublished - Apr 1981


  • Acetylcholinesterase
  • Aminopeptidase
  • Puromycin analogs

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience


Dive into the research topics of 'Inhibition of Aminopeptidase and Acetylcholinesterase by Puromycin and Puromycin Analogs'. Together they form a unique fingerprint.

Cite this