Fraction of acetylcholinesterase (AChE) polypeptides that are degraded within an hour of synthesis in chick muscle cells

Range >80 % of polypeptides
Organism Chicken Gallus gallus
Reference Massoulié J, Pezzementi L, Bon S, Krejci E, Vallette FM. Molecular and cellular biology of cholinesterases. Prog Neurobiol. 1993 Jul41(1):31-91 p.60 right column bottom paragraphPubMed ID8321908
Primary Source Rotundo RL. Biogenesis of acetylcholinesterase molecular forms in muscle. Evidence for a rapidly turning over, catalytically inactive precursor pool. J Biol Chem. 1988 Dec 25 263(36):19398-406.PubMed ID3198632
Method P.60 right column bottom paragraph: "The metabolism of both inactive and active AChE in chick muscle cells has also been studied by radioactive incorporation (primary source). In these experiments, immunoprecipitation was used to follow the synthesis of AChE associated protein."
Comments P.60 right column bottom paragraph: "The results showed that over 80% of the AChE polypeptides were degraded within 1 hr, without becoming catalytically active."
Entered by Uri M
ID 115066