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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1991-3-7
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pubmed:abstractText |
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. The oligosaccharides were isolated by gel permeation chromatography and their structures determined by 500-MHz 1H NMR spectroscopy, fast atom bombardment-mass spectrometry, and high-pH anion-exchange chromatography. The high-mannose oligosaccharides Man5GlcNAc2, Man6GlcNAc2, Man7GlcNAc2, Man8GlcNAc2, and Man9GlcNAc2 were present in the ratios 2:49:19:24:6 and accounted for all the asparagine-linked oligosaccharides released from Art v II by PNGase F. The NH2-terminal amino acid sequences of Art v II and of four peptides generated by cyanogen bromide (CNBr) cleavage of deglycosylated Art v II were determined. The first 30 amino acid residues of Art v II did not contain any potential N-glycosylation sites. One potential N-glycosylation site was identified in one of the CNBr fragments. The native protein conformation was shown by enzyme-linked immunosorbent assay inhibition assays to be essential for the binding of rabbit IgG to Art v II and for the binding of human IgE to the major IgE-binding epitope(s) in this allergen. At least one minor IgE-binding epitope still bound IgE after denaturation of the allergen. Removal of the high-mannose chains from denatured Art v II had no significant effect on the binding of human IgE to the minor IgE-binding epitope(s).
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Allergens,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Asparagine,
http://linkedlifedata.com/resource/pubmed/chemical/Cyanogen Bromide,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/allergen Art v II protein...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2660-8
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:1703533-Allergens,
pubmed-meshheading:1703533-Amino Acid Sequence,
pubmed-meshheading:1703533-Animals,
pubmed-meshheading:1703533-Antigens, Plant,
pubmed-meshheading:1703533-Asparagine,
pubmed-meshheading:1703533-Carbohydrate Sequence,
pubmed-meshheading:1703533-Chromatography, Gel,
pubmed-meshheading:1703533-Chromatography, Ion Exchange,
pubmed-meshheading:1703533-Cyanogen Bromide,
pubmed-meshheading:1703533-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:1703533-Epitopes,
pubmed-meshheading:1703533-Glycoproteins,
pubmed-meshheading:1703533-Glycoside Hydrolases,
pubmed-meshheading:1703533-Immunoglobulin G,
pubmed-meshheading:1703533-Magnetic Resonance Spectroscopy,
pubmed-meshheading:1703533-Molecular Sequence Data,
pubmed-meshheading:1703533-Oligosaccharides,
pubmed-meshheading:1703533-Plant Proteins,
pubmed-meshheading:1703533-Plants,
pubmed-meshheading:1703533-Pollen,
pubmed-meshheading:1703533-Protein Conformation,
pubmed-meshheading:1703533-Rabbits
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pubmed:year |
1991
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pubmed:articleTitle |
Structural analysis of the glycoprotein allergen Art v II from the pollen of mugwort (Artemisia vulgaris L.).
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pubmed:affiliation |
Department of Pharmacy, University of Oslo, Norway.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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