Open AccessIn-cell matrix-assisted laser desorption-ionization fourier transform ion cyclotron resonance mass spectrometry
Author(s) -
M. Knobeler,
K.P. Wanczek
Publication year - 1996
Publication title -
journal of the american society for mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.961
H-Index - 127
eISSN - 1879-1123
pISSN - 1044-0305
DOI - 10.1016/1044-0305(96)00029-3
Subject(s) - fourier transform ion cyclotron resonance , chemistry , mass spectrometry , ion cyclotron resonance , analytical chemistry (journal) , ionization , top down proteomics , ion , matrix assisted laser desorption/ionization , selected ion monitoring , atomic physics , desorption , protein mass spectrometry , cyclotron , tandem mass spectrometry , chromatography , physics , gas chromatography–mass spectrometry , organic chemistry , adsorption
A new internal matrix-assisted laser desorption-ionization (MALDI) Fourier transform ion cyclotron resonance-mass spectrometry (FTICR-MS) method is introduced. The target is directly positioned at one trapping electrode of a single cylindrical ion cyclotron resonance (ICR) cell and becomes a part of it. The ionization occurs inside the ICR cell in contrast to external or near-cell MALDI-FTICR-MS techniques. Very efficient trapping and mass resolving power better than unit resolution of singly charged peptides and proteins ions up to 2000 u is possible by using only basic FTICR-MS techniques. The sole application of a pulsed retarding potential increases the mass range to 6000 u. No collisional cooling and quadrupolar excitation was done. Sensitivities below 1 fmol, and ion storage times of more than 15 s are shown. High resolving powers of 16,000 and 56,000 are obtained on bovine insulin (5.7 ku) and gramicidin D (1.9 ku), respectively.