Mass spectrometric studies on the N-linked oligosaccharides of baculovirus-expressed mouse interleukin-3.

A combination of mass spectrometry techniques, high-pH anion-exchange chromatography and enzymatic digestions has been applied to elucidate the structures of the N-linked oligosaccharides on baculovirus-expressed mouse interleukin-3 produced in Bombyx mori larvae. This recombinant lymphokine was found to be heterogeneously glycosylated with mannosidic chitobiose core type oligosaccharides. A single N-linked oligosaccharide with the truncated structure of Man alpha 1-6Man beta 1-4GlcNAc1-4(Fuc alpha 1-6)GlcNAc was found to be the predominant species.