| Either high-mannose-type or hybrid-type oligosaccharide is linked to the same asparagine residue in ovalbumin. | |
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MedLine Citation:
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PMID: 7284436 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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After pepsin digestion, all of the carbohydrates in ovalbumin were recovered in two glycopeptides, Glu-Glu-Lys-Tyr-Asn(CHO)-Leu-Thr-Ser-Val and Glu-Gln-Lys-Tyr-Asn(CHO)-Leu-Thr-Ser-Val. Almond glycopeptidase released quantitatively oligosaccharides from the glycopeptides. The products from both glycopeptides contained both the high-mannose-type oligosaccharides and the hybrid-type oligosaccharides in the same ratio. Thus, either the high-mannose-type or the hybrid-type oligosaccharide is attached to the unique asparagine residue in the ovalbumin molecule. |
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Authors:
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H Ishihara; N Takahashi; J Ito; E Takeuchi; S Tejima |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 669 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 1981 Jul |
Date Detail:
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Created Date: 1981-12-15 Completed Date: 1981-12-15 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 216-21 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amidohydrolases Animals Asparagine* Chickens Glycopeptides Mannose / analysis Oligosaccharides / analysis* Ovalbumin* Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Plants / enzymology |
| Chemical | |
Reg. No./Substance:
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0/Glycopeptides; 0/Oligosaccharides; 31103-86-3/Mannose; 7006-34-0/Asparagine; 9006-59-1/Ovalbumin; EC 3.5.-/Amidohydrolases; EC 3.5.1.52/Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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