SURFACES FOR INTERFACING PROTEIN GEL-ELECTROPHORESIS DIRECTLY WITH MASS-SPECTROMETRY

Citation
Mm. Vestling et C. Fenselau, SURFACES FOR INTERFACING PROTEIN GEL-ELECTROPHORESIS DIRECTLY WITH MASS-SPECTROMETRY, Mass spectrometry reviews, 14(3), 1995, pp. 169-178
Citations number
69
Language
INGLESE
art.tipo
Review
Categorie Soggetti
Spectroscopy
Journal title
ISSN journal
0277-7037
Volume
14
Issue
3
Year of publication
1995
Pages
169 - 178
Database
ISI
SICI code
0277-7037(1995)14:3<169:SFIPGD>2.0.ZU;2-G
Abstract
Molecular biologists and biochemists often transfer proteins separated by gel electrophoresis to membranes, such as PVDF (polyvinylidene dif luoride) and nitrocellulose, for further characterization. MALDI-MS (m atrix-assisted laser desorption/ionization mass spectrometry) can anal yze proteins and peptides on a wide variety of surfaces. This review s urveys the suitability of membranes and surfaces used by molecular bio logists and biochemists as mass spectrometric surfaces. Matrix applica tion considerations are reviewed. The identification of proteins by co mparing the masses of peptides generated by on-membrane digestion of p roteins with theoretical digestion of database proteins is discussed. The prospects for mass spectrometric sequencing of individual peptides on membranes are presented. (C) 1996 John Wiley & Sons, Inc.