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.
|Number of pages||3|
|Journal||Journal of Neurochemistry|
|State||Published - Apr 1981|
- Puromycin analogs
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience