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.
Hogeland
K E
KE
Department of Chemistry, Oregon State University, Corvallis 97331.
Deinzer
M L
ML
D000595:Amino Acid Sequence; D000818:Animals; D016367:Baculoviridae / Q000235:genetics*; D012831:Bombyx / Q000378:metabolism; D002240:Carbohydrate Sequence; D007377:Interleukin-3 / Q000737:chemistry / Q000235:genetics*; D013058:Mass Spectrometry; D051379:Mice; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry*
D007377:Interleukin-3; D009844:Oligosaccharides