N-Linked glycans derived from human and bovine
1-acidglycoprotein, as well as chicken egg white albumin, wereanalyzed by MALDI-TOF mass spectrometry using a novelMALDI matrix consisting of 2,5-dihydroxybenzoic acid(DHB) and aniline. A significant increase in signal wasobserved for these oligosaccharides relative to the signalobtained when unmodified DHB was used as a matrix forthe same set of samples. The use of aniline/DHB matrixalso led to facile on-target derivatization of the glycans vianonreductive amination, as aniline was found to form astable Schiff base with the reducing end GlcNAc residuewithout the need for prolonged incubation periods andelevated temperatures. Both native and derivatized glycans ionized as sodium adducts and had similar MS/MSfragmentation patters consisting mainly of Y/B-cleavageions. In our experiments, we obtained evidence forpersistence of the derivatization reaction in the solidphase; i.e., the reaction appeared to be taking place evenafter the sample-matrix spot had dried. This is the firstreport on such solid-phase on-target derivatization ofcarbohydrates for subsequent analysis by MALDI massspectrometry.