Structural analysis of the glycoprotein allergen Art v II from the pollen of mugwort (Artemisia vulgaris L.).
作者： B M Nilsen , K Sletten , B S Paulsen , M O'Neill , H van Halbeek
DOI: 10.1016/S0021-9258(18)52295-X
关键词: Cyanogen bromide 、 Biochemistry 、 Mugwort 、 PNGase F 、 Chemistry 、 Epitope 、 Amino acid 、 Denaturation (biochemistry) 、 Gel permeation chromatography 、 Peptide
摘要: The glycoprotein allergen Art v II, from the pollen of mugwort (Artemisia vulgaris L.) was treated with peptide:N-glycosidase F (PNGase F) to release asparagine-linked oligosaccharides. oligosaccharides were isolated by gel permeation chromatography and their structures determined 500-MHz 1H NMR spectroscopy, fast atom bombardment-mass spectrometry, high-pH anion-exchange chromatography. high-mannose Man5GlcNAc2, Man6GlcNAc2, Man7GlcNAc2, Man8GlcNAc2, Man9GlcNAc2 present in ratios 2:49:19:24:6 accounted for all released II PNGase F. NH2-terminal amino acid sequences four peptides generated cyanogen bromide (CNBr) cleavage deglycosylated determined. first 30 residues did not contain any potential N-glycosylation sites. One site identified one CNBr fragments. native protein conformation shown enzyme-linked immunosorbent assay inhibition assays be essential binding rabbit IgG human IgE major IgE-binding epitope(s) this allergen. At least minor epitope still bound after denaturation Removal chains denatured had no significant effect on epitope(s).
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