REJTAR, Tomas, Hu PING, Peter JUHASZ, Jennifer M. CAMPBELL, Marvin L. VESTAL, Jan PREISLER and Barry, L. KARGER. Off-Line Coupling of High-Resolution Capillary Electrophoresis to MALDI-TOF and TOF/TOF MS. Journal of Proteome Research. Washington, USA: ACS, 2002, vol. 1, No 2, p. 171-179. ISSN 1535-3893.
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Basic information
Original name Off-Line Coupling of High-Resolution Capillary Electrophoresis to MALDI-TOF and TOF/TOF MS
Authors REJTAR, Tomas (203 Czech Republic), Hu PING (156 China), Peter JUHASZ (840 United States of America), Jennifer M. CAMPBELL (840 United States of America), Marvin L. VESTAL (840 United States of America), Jan PREISLER (203 Czech Republic, guarantor) and Barry, L. KARGER (840 United States of America).
Edition Journal of Proteome Research, Washington, USA, ACS, 2002, 1535-3893.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10406 Analytical chemistry
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
RIV identification code RIV/00216224:14310/02:00008546
Organization unit Faculty of Science
UT WoS 000178238600008
Keywords in English MALDI; mass spectrometry; capillary electrophoresis; proteomics; proteins; peptides; interface;
Tags Capillary electrophoresis, interface, MALDI, mass spectrometry, peptides, proteins, proteomics
Changed by Changed by: prof. Mgr. Jan Preisler, Ph.D., učo 45329. Changed: 27/6/2009 23:58.
Abstract
High-resolution capillary electrophoresis has been coupled to MALDI-TOF and TOF/TOF MS through off-line vacuum deposition onto standard stainless steel MALDI targets. This off-line approach allowed the decoupling of the separation from the MS analysis, thus allowing each to be independently optimized in terms of time. Using BSA tryptic digest as a model sample, the deposited streaks, roughly 100-ím wide, were first analyzed in the MS mode, consuming only a fraction of the sample. After data analysis, segments of the deposited trace, containing unidentified peptides, as well as several species chosen for sequence confirmation, were reanalyzed in the MS/MS mode using MALDI-TOF/TOF MS. Additionally, it is shown that the shot-to-shot reproducibility of the vacuum-deposited trace (5% RSD) is 1 order of magnitude lower than that found for the standard dried droplet method. Moreover, a linear dependence of signal intensities (relative to an internal standard) over 3 orders of magnitude was found for a peptide sample with concentrations ranging from 1 to 1000 nM. This paper demonstrates the potential of off-line coupling of high-resolution separations to MALDI-MS and MALDI-MS/MS using vacuum deposition for the analysis of complex peptide mixtures from protein digests.
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