| pubmed-article:1703533 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1703533 | lifeskim:mentions | umls-concept:C0002092 | lld:lifeskim |
| pubmed-article:1703533 | lifeskim:mentions | umls-concept:C0032385 | lld:lifeskim |
| pubmed-article:1703533 | lifeskim:mentions | umls-concept:C0348066 | lld:lifeskim |
| pubmed-article:1703533 | lifeskim:mentions | umls-concept:C0524798 | lld:lifeskim |
| pubmed-article:1703533 | lifeskim:mentions | umls-concept:C0003826 | lld:lifeskim |
| pubmed-article:1703533 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
| pubmed-article:1703533 | lifeskim:mentions | umls-concept:C0078059 | lld:lifeskim |
| pubmed-article:1703533 | lifeskim:mentions | umls-concept:C0204514 | lld:lifeskim |
| pubmed-article:1703533 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:1703533 | pubmed:dateCreated | 1991-3-7 | lld:pubmed |
| pubmed-article:1703533 | 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). | lld:pubmed |
| pubmed-article:1703533 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1703533 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1703533 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1703533 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1703533 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1703533 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1703533 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1703533 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1703533 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1703533 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1703533 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1703533 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1703533 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1703533 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1703533 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1703533 | pubmed:author | pubmed-author:SlettenKK | lld:pubmed |
| pubmed-article:1703533 | pubmed:author | pubmed-author:O'NeillMM | lld:pubmed |
| pubmed-article:1703533 | pubmed:author | pubmed-author:PaulsenB SBS | lld:pubmed |
| pubmed-article:1703533 | pubmed:author | pubmed-author:van HalbeekHH | lld:pubmed |
| pubmed-article:1703533 | pubmed:author | pubmed-author:NilsenB MBM | lld:pubmed |
| pubmed-article:1703533 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1703533 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:1703533 | pubmed:volume | 266 | lld:pubmed |
| pubmed-article:1703533 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1703533 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1703533 | pubmed:pagination | 2660-8 | lld:pubmed |
| pubmed-article:1703533 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:1703533 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1703533 | pubmed:articleTitle | Structural analysis of the glycoprotein allergen Art v II from the pollen of mugwort (Artemisia vulgaris L.). | lld:pubmed |
| pubmed-article:1703533 | pubmed:affiliation | Department of Pharmacy, University of Oslo, Norway. | lld:pubmed |
| pubmed-article:1703533 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1703533 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1703533 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:1703533 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1703533 | lld:pubmed |
