Premium
Hydrophobic labeling of the membrane binding domain of acetylcholinesterase from Torpedo marmorata
Author(s) -
Stieger S.,
Brodbeck U.,
Reber B.,
Brunner J.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80252-5
Subject(s) - torpedo , acetylcholinesterase , chemistry , membrane , domain (mathematical analysis) , biophysics , biochemistry , biology , enzyme , acetylcholine receptor , receptor , mathematics , mathematical analysis
Membrane‐bound acetylcholinesterase (AChE) from the electric organ of Torpedo marmorata was labeled with the hydrophobic photoactivatable reagent 3‐trifluoromethyl‐3‐( m ‐[ 125 I]iodophenyl)diazirine ([ 125 I]TID). Labeling with [ 125 I]TID was restricted to the membranous polypeptide segment of AChE as shown upon conversion of the amphiphilic form to the hydrophilic one by limited digestion with proteinase K. The labeled membranous segment, which has an M r of approx. 3000 was isolated by gel filtration on Sephadex LH‐60 in ethanol/formic acid.