The membrane anchor of mammalian brain acetylcholinesterase consists of a single glycosylated protein of 22 kDa

被引：20

作者：

Boschetti, N ^{[1
]}

Brodbeck, U ^{[1
]}

机构：

[1] UNIV BERN, INST BIOCHEM & MOLEC BIOL, CH-3012 BERN, SWITZERLAND

来源：

FEBS LETTERS | 1996年 / 380卷 / 1-2期

关键词：

acetylcholinesterase; hydrophobic label; membrane anchor; brain; amino acid sequence;

D O I：

10.1016/0014-5793(96)00041-5

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：

Mammalian brain acetylcholinesterase (AChE; EC 3.1.1.7) is membrane-bound through a structural subunit of about 20 kDa. So far little is known about this anchor because it is only detectable after hydrophobic labelling. In the present study we demonstrate that the two bands migrating around 20 kDa on SDS-PAGE derive from the same protein containing the same N-terminal amino acid sequence. The difference in their mobility is due to different N-glycosidation. Radioalkylation of cysteine residues reveals that the anchor contains just the two cysteine residues involved in binding the catalytic subunits.

引用

页码：133 / 136

页数：4

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