PHOTOAFFINITY LABELING AND QUATERNARY STRUCTURE OF ACETYLCHOLINE-RECEPTOR FROM TORPEDO-CALIFORNICA

被引：73
作者：
HUCHO, F
LAYER, P
KIEFER, HR
BANDINI, G
机构：
[1] UNIV KONSTANZ, FACHBEREICH BIOL, D-7750 KONSTANZ, FED REP GER
[2] BASEL INST IMMUNOL, BASEL 5, SWITZERLAND
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1976年 / 73卷 / 08期
关键词：
D O I：
10.1073/pnas.73.8.2624
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Membrane fragments from electric tissue of Torpedo californica containing nicotinic acetylcholine receptor were composed of 4 different polypeptide chains with MW of 40,000 (.alpha.), 48,000 (.beta.), 62,000 (.gamma.) and 66,000 (.delta.). The .alpha. and .beta. chains were still present in all and .gamma. and .delta. in some of the receptor preparations after Triton X-100 extraction and purification by affinity chromatography. All components of the receptor reacted covalently with the photoaffinity label 4-azido-2-nitrobenzyltrimethylammonium fluoroborate, the .delta. chain incorporating less of the reagent compared to the .alpha. and .beta. chains. Agonists and antagonists containing a quaternary ammonium group protected all chains against the label; the principal neurotoxin from Naja naja siamensis protected the .alpha. chain only. The .alpha. chain apparently binds the neurotoxin from Naja naja, and the .alpha. and .beta. chains are involved in the binding of ligands with quaternary ammonium groups. The function of the .gamma. and .delta. chains remains to be determined.
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页码：2624 / 2628
页数：5
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