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Cesium ion liquid secondary ion mass spectrometry of membrane‐bound glycoproteins: Structural and topological considerations of acetylcholine receptor from Torpedo californica
Author(s) -
Poulter L.,
Earnest J. P.,
Stroud R. M.,
Burlingame A. L.
Publication year - 1988
Publication title -
biomedical and environmental mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0887-6134
DOI - 10.1002/bms.1200160105
Subject(s) - chemistry , mass spectrometry , chromatography , fragmentation (computing) , torpedo , secondary ion mass spectrometry , ion , nicotinic acetylcholine receptor , glycoprotein , membrane , analytical chemistry (journal) , acetylcholine receptor , receptor , biochemistry , organic chemistry , biology , ecology
Abstract We report mass mapping of a large (270 kD) multisubunit membrane bound glycoprotein, nicotinic acetylcholine receptor from Torpedo californica , using enzymic digests of the affinity purified whole receptor and cesium ion liquid secondary ion mass spectrometry. Peptides, glycopeptides and derivatized N‐linked oligosaccharides were isolated by HPLC and identified by LSIMS. We have shown that mass spectrometric sensitivity is improved a hundred‐fold through use of computer‐controlled mass window stepping of an electro‐optical multichannel array detection system on a LSIMS double focusing mass spectrometer. This new method permitted determination of the complete fragmentation pattern of Man 8 N 2 ‐ABEE using only 5 picomoles of sample.