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Spin‐coated samples for high resolution matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry of large proteins
Author(s) -
Perera Indral K.,
Perkins John,
Kantartzoglou Stamatina
Publication year - 1995
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290090215
Subject(s) - chemistry , mass spectrometry , analyte , analytical chemistry (journal) , mass spectrum , resolution (logic) , time of flight mass spectrometry , matrix assisted laser desorption electrospray ionization , matrix assisted laser desorption/ionization , laser , matrix (chemical analysis) , biomolecule , polyatomic ion , ionization , ion , desorption , maldi imaging , chromatography , optics , adsorption , biochemistry , physics , organic chemistry , artificial intelligence , computer science
The preparation of near homogeneous samples of large biomolecules, based on the method of spin coating sample substrates, and their use in matrix‐assisted laser/desorption ionization mass spectrometry, for generating spectra with highly reproducible ion signals of analyte molecules with mass extending up to about 150 000 u, are reported. These samples, which could easily be reproduced, consisted of a uniform distribution of matrix/analyte microcrystals over the entire sample surface. Upon laser irradiation, they provided enhanced molecular ion yields and thereby allowed the acquisition of good quality mass spectra over a few (∼1–5) laser pulses. Methods for improving the mass resolution of the molecular ion signals were examined, and a spectrum of bovine insulin obtained from a linear time‐of‐flight instrument with a mass resolution in excess of 1450, together with one of chicken egg lysozyme displaying a resolution of about 450, are presented. The influence of the matrix/analyte molar ratio on the molecular ion yield has also been studied.