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.