2002
Capillary Array Electrophoresis-MALDI Mass Spectrometry Using a Vacuum Deposition Interface
PREISLER, Jan, Ping HU, Barry, L. KARGER, Tomáš REJTAR, Eugene MOSKOVEETS et. al.Základní údaje
Originální název
Capillary Array Electrophoresis-MALDI Mass Spectrometry Using a Vacuum Deposition Interface
Autoři
PREISLER, Jan (203 Česká republika, garant), Ping HU (156 Čína), Barry, L. KARGER (840 Spojené státy), Tomáš REJTAR (203 Česká republika) a Eugene MOSKOVEETS (643 Rusko)
Vydání
Analytical Chemistry, Washington, D.C., USA, American Chemical Society, 2002, 0003-2700
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10406 Analytical chemistry
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Impakt faktor
Impact factor: 5.094
Kód RIV
RIV/00216224:14310/02:00008542
Organizační jednotka
Přírodovědecká fakulta
UT WoS
000173086200010
Klíčová slova anglicky
capillary array electrophoresis; MALDI; mass spectrometry; proteomics; peptide
Změněno: 28. 6. 2009 00:01, prof. Mgr. Jan Preisler, Ph.D.
Anotace
V originále
The approach of vacuum deposition has been extended to demonstrate parallel analysis for multiple on-line infusion MALDI TOF MS and capillary array electrophoresis (CAE)-MALDI MS. In the infusion mode, individual peptide samples were simultaneously deposited on a Mylar tape cartridge using an array of eight capillaries, yielding eight parallel traces. For CAE-MALDI/TOF MS, the same number of separation capillaries were coupled with an array of eight infusion capillaries using a common liquid junction, containing matrix solution. A fast-scanning mirror was employed to traverse the beam of the desorption laser across the Mylar tape to probe one trace at a time. The positions of the eight sample traces formed on the tape were automatically determined, and all samples were analyzed in rapid sequence using a kilohertz repetition rate laser and a high-throughput data acquisition system. The instrumentation was operated with CAE MS for high-throughput analysis without compromising data quality applicable to MALDI/TOF MS analysis for proteomics and other areas where separation and high throughput are required.