Glutathione as a matrix for plasma desorption mass spectrometry of large peptides.
Glutathione as a matrix for plasma desorption mass spectrometry of large peptides.
复制标题
谷胱甘肽作为大肽等离子体解吸质谱分析的基质。
DOI:
10.1021/ac00298a008
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发表时间:
1986
影响因子:
7.4
通讯作者:
Robert J. Cotter
中科院分区:
文献类型:
--
作者:
M. Alai;P. Demirev;Catherine Fenselau;Robert J. Cotter
The plasma desorption mass spectra of large peptides, dissolved and electrosprayed In solutions containing glutathione, show Increased molecular Ion signal, reduction of base-line noise and peak widths, and an Increase In multiply charged Ions. The reduced, rather than the oxidized, form of gluta-thione Is responsible for these effects. Some other chemically similar matrices show similar effects while others do not. Several roles for the matrix are suggested Including previously reported effects on protein refolding and aggregation In solution, as well as possibilities for lowering the sample/substrate binding energy during desorption.The importance of appropriate chemical/physical matrices for the desorption of intractable compounds in mass spec-trometry was underscored by the introduction of glycerol (1, 2), as an integral part of the fast atom bombardment technique. From the beginning it was understood that the liquid matrix providedstrong stable secondary ion signals under high-flux bombardment necessary for high-performance double-focusing mass spectrometers capable of high-mass ranges (3). More recently, the possibility for reducing the internal energy of secondary ions by solvent shedding has also been suggested (4, 5). The addition of acid to glycerol or the use of monothioglycerol improves the matrix’s role as a proton donor (3, 6). Other matrices, such as tetraglyme for cesium perfluoroalkonate clusters (6), or mixtures of thiols, such as dithiothreitol and dithioerythritol forpeptides (7), havebeen
影响因子:
7.4
作者:
Ackermann,BL;Watson,JT;Holland,JF
通讯作者:
Holland,JF