STRUCTURAL LOCALIZATION OF THE SEQUENCE-ALPHA235-242 OF THE NICOTINIC ACETYLCHOLINE-RECEPTOR

被引：24

作者：

CRIADO, M ^{[1
]}

SARIN, V ^{[1
]}

FOX, JL ^{[1
]}

LINDSTROM, J ^{[1
]}

机构：

[1] ABBOTT LABS, DEPT MOLEC BIOL, N CHICAGO, IL 60064 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1985年 / 128卷 / 02期

关键词：

D O I：

10.1016/0006-291X(85)90126-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Two monoclonal antibodies (mAb 254 and 255) were obtained against a synthetic peptide corresponding to the sequence 235-242 of the .alpha.-subunit of Torpedo acetylcholine receptor. These mAbs could bind to receptor in native membrane vesicles only when these vesicles were permeabilized, suggesting that the sequence .alpha.235-242 is exposed on the cytoplasmic surface of the receptor. Further evidence for the cytoplasmic localization of this sequence was partial competition for binding between these mAbs and mAbs previously demonstrated to bind to the cytoplasmic part of the receptor. A model is proposed which accounts for all the experimental data obtained this far on the transmembrane orientation of the subunit polypeptide chains.

引用

页码：864 / 871

页数：8

共 25 条

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