Enzymatic carboxymethylation of the nicotinic acetylcholine receptor

Yoel Kloog*, Donna Flynn, Andrew R. Hoffman, Julius Axelrod

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

35 Scopus citations

Abstract

The enzymatic carboxymethylation of the acetylcholine receptors isolated from Torpedo california is described. The acetylcholine receptor was found to be one of the most active substrates for protein carboxymethylase. The receptor methylation is not affected by the binding of cholinergic ligand. Purification of protein methyl acceptor activity from membranes of electric organ paralleled that of enrichment of the acetylcholine receptor. The enzyme which catalyzes the reaction, protein carboxymethylase, was found in the Torpedo electric organ. The enzyme from the Torpedo electric organ is mainly located in the cytosol and has high affinity for the methyl donor S-adenosyl-L-methionine and for the nicotinic acetylcholine receptor protein.

Original languageEnglish
Pages (from-to)1474-1480
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume97
Issue number4
DOIs
StatePublished - 31 Dec 1980
Externally publishedYes

Funding

FundersFunder number
Hoffmann LaRoche Co.
National Institutes of Health
U.S. Public Health ServiceF05 TWO 2811-01, NS 14651

    Keywords

    • AcChoR
    • PCM
    • S-adenosylhomocysteine
    • S-adenosylmethionine
    • SAH
    • SAM
    • TCA
    • nicotinic acetylcholine receptor protein
    • protein carboxymethylase
    • trichloro acetic acid

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