@article{8e9f1be8d94846259f642d1e22b68f5b,
title = "Enzymatic carboxymethylation of the nicotinic acetylcholine receptor",
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.",
keywords = "AcChoR, PCM, S-adenosylhomocysteine, S-adenosylmethionine, SAH, SAM, TCA, nicotinic acetylcholine receptor protein, protein carboxymethylase, trichloro acetic acid",
author = "Yoel Kloog and Donna Flynn and Hoffman, {Andrew R.} and Julius Axelrod",
note = "Funding Information: This research was supported in part by a grant from the National Institutes of Health (U.S. Public Health Service NS 14651). Y.K. was supported by U.S. Public Health Service International Research Fellowship F05 TWO 2811-01 and a stipend from Hoffmann LaRoche Co. The authors thank Dr. V. Manganiello for the gift of calmodulin and Dr. M. Sokolovsky and Dr. D.M. Michaelson for the gift of electric organ tissue.",
year = "1980",
month = dec,
day = "31",
doi = "10.1016/S0006-291X(80)80031-3",
language = "אנגלית",
volume = "97",
pages = "1474--1480",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Elsevier B.V.",
number = "4",
}