Hydrophobic labeling of the membrane binding domain of acetylcholinesterase from Torpedo marmorata

FEBS Letters

Brodbeck, U.¹  Reber, B.²  Stieger, S.¹  Brunner, J.² 

[1] Medizinisch-chemisches Institut der Universität Bern, Bühlstrasse 28, CH-3000 Bern 9 Switzerland;Laboratorium für Biochemie der ETH Zürich, Universitätsstrasse 16, CH-8092 Zürich, Switzerland

关键词: Acetylcholinesterase;    Torpedo marmorata;    Membrane protein;    Hydrophobic labeling;    Proteolytic digestion;    Anchor peptide;    AChE;    acetylcholinesterase;    [125I]TID;    3-trifluoromethyl-3-(m-[125I]iodophenyl)diazirine;   

DOI  :  10.1016/0014-5793(84)80252-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Membrane-bound acetylcholinesterase (AChE) from the electric organ of Torpedo marmorata was labeled with the hydrophobic photoactivatable reagent 3-trifluoromethyl-3-(m-[¹²⁵I]iodophenyl)diazirine ([¹²⁵I]TID). Labeling with [¹²⁵I]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.

【 授权许可】

Unknown