ANIONIC SUBSITES OF THE ACETYLCHOLINESTERASE FROM TORPEDO-CALIFORNICA - AFFINITY LABELING WITH THE CATIONIC REAGENT N,N-DIMETHYL-2-PHENYL-AZIRIDINIUM

被引：83

作者：

WEISE, C ^{[1
]}

KREIENKAMP, HJ ^{[1
]}

RABA, R ^{[1
]}

PEDAK, A ^{[1
]}

AAVIKSAAR, A ^{[1
]}

HUCHO, F ^{[1
]}

机构：

[1] ACAD SCI ESSSR,DEPT BIOCHEM,INST CHEM PHYS & BIOPHYS,200103 TALLINN,ESTONIA,USSR

来源：

EMBO JOURNAL | 1990年 / 9卷 / 12期

关键词：

acetylcholinesterase; affinity labelling; anionic subsite; N; N-dimethyl-2-phenyl-aziridinium;

D O I：

10.1002/j.1460-2075.1990.tb07607.x

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：

Several peptides of acetylcholinesterase of Torpedo californica labelled with the alkylating reagent [3H]N,N-dimethyl-2-phenyl-aziridinium (DPA) were localized within the primary structure. One peptide had the sequence KPQELIDVE (positions 270-278); the incorporation of DPA into this peptide could be specifically suppressed by propidium, which suggests that it is part of the peripheral anionic site. The incorporation of DPA into two other peptides was insensitive to propidium but could be prevented by edrophonium; the sequence of one of the peptides assumed to be part of the anionic site in the catalytic centre was found to be DLFR (positions 217-220). Decamethonium efficiently blocked alkylating by DPA in all three investigated peptides.

引用

页码：3885 / 3888

页数：4

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