J 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.

Basic information

Original name

Capillary Array Electrophoresis-MALDI Mass Spectrometry Using a Vacuum Deposition Interface

Authors

PREISLER, Jan (203 Czech Republic, guarantor), Ping HU (156 China), Barry, L. KARGER (840 United States of America), Tomáš REJTAR (203 Czech Republic) and Eugene MOSKOVEETS (643 Russian Federation)

Edition

Analytical Chemistry, Washington, D.C., USA, American Chemical Society, 2002, 0003-2700

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10406 Analytical chemistry

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 5.094

RIV identification code

RIV/00216224:14310/02:00008542

Organization unit

Faculty of Science

UT WoS

000173086200010

Keywords in English

capillary array electrophoresis; MALDI; mass spectrometry; proteomics; peptide
Změněno: 28/6/2009 00:01, prof. Mgr. Jan Preisler, Ph.D.

Abstract

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.