Enzymatic methylation of the membrane-bound nicotinic acetylcholine receptor.

D. D. Flynn*, Y. Kloog, L. T. Potter, J. Axelrod

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

The acetylcholine receptor of the Torpedo electric organ acts as substrate for the enzyme protein carboxyl methyltransferase within receptor-enriched membranes and after it is purified. In right-side-out receptor-enriched vesicles, protein of the membrane. All four receptor subunits were found to be methylated from the inside as well outside of the membrane vesicles. The higher molecular weight subunits were found to be methylated to a greater degree than the lower molecular weight subunits.

Original languageEnglish
Pages (from-to)9513-9517
Number of pages5
JournalJournal of Biological Chemistry
Volume257
Issue number16
StatePublished - 25 Aug 1982

Funding

FundersFunder number
National Heart, Lung, and Blood InstituteT32HL007188

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