Source:http://linkedlifedata.com/resource/pubmed/id/10091584
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
1999-4-22
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| pubmed:abstractText |
Zona pellucida, a transparent envelope surrounding the mammalian oocyte, plays important roles in fertilization and consists of three glycoproteins; ZPA, ZPB and ZPC. In pig, neutral complex-type N-linked chains obtained from a ZPB/ZPC mixture possess sperm-binding activity. We have recently reported that among neutral N-linked chains triantennary and tetraantennary chains have a sperm-binding activity stronger than that of diantennary chains. Triantennary and tetraantennary chains are localized at the second of the three N-glycosylation sites of ZPB. In this study, we focused on the localization of neutral N-linked chains in ZPC. ZPB and ZPC can not be separated from each other unless the acidic N-acetyllactosamine regions of their carbohydrate chains are removed by endo-beta-galactosidase digestion. A large part of the acidic N-linked chains becomes neutral by the digestion, but the main neutral N-linked chains are not susceptible to the enzyme. N-glycanase digestion indicated that ZPC has three N-glycosylation sites. Three glycopeptides each containing one of the N-glycosylation sites were obtained by tryptic digestion of ZPC and the N-glycosylation sites were revealed as Asn124, Asn146 and Asn271. The carbohydrate structures of the neutral N-linked chains from each glycopeptide were characterized by two-dimensional sugar mapping analysis taking into consideration the structures of the main, intact neutral N-linked chains of ZPB/ZPC mixture reported previously. Triantennary and tetraantennary chains were found mainly at Asn271 of ZPC, whereas diantennary chains were present at all three N-glycosylation sites. Thus, ZPC has tri-antennary and tetra-antennary chains as well as ZPB, but the localization of the chains is different from that in ZPB.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amidohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Egg Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide-N4-(N-acetyl-beta-glucosamin...,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase,
http://linkedlifedata.com/resource/pubmed/chemical/keratan-sulfate...,
http://linkedlifedata.com/resource/pubmed/chemical/zona pellucida glycoproteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0014-2956
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
260
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
57-63
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| pubmed:dateRevised |
2007-7-23
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| pubmed:meshHeading |
pubmed-meshheading:10091584-Amidohydrolases,
pubmed-meshheading:10091584-Animals,
pubmed-meshheading:10091584-Carbohydrate Sequence,
pubmed-meshheading:10091584-Egg Proteins,
pubmed-meshheading:10091584-Female,
pubmed-meshheading:10091584-Glycopeptides,
pubmed-meshheading:10091584-Glycoside Hydrolases,
pubmed-meshheading:10091584-Glycosylation,
pubmed-meshheading:10091584-Membrane Glycoproteins,
pubmed-meshheading:10091584-Molecular Sequence Data,
pubmed-meshheading:10091584-Oligosaccharides,
pubmed-meshheading:10091584-Oocytes,
pubmed-meshheading:10091584-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase,
pubmed-meshheading:10091584-Receptors, Cell Surface,
pubmed-meshheading:10091584-Swine,
pubmed-meshheading:10091584-Trypsin,
pubmed-meshheading:10091584-Zona Pellucida,
pubmed-meshheading:10091584-beta-Galactosidase
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| pubmed:year |
1999
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| pubmed:articleTitle |
Localization of neutral N-linked carbohydrate chains in pig zona pellucida glycoprotein ZPC.
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| pubmed:affiliation |
Graduate School of Science and Technology, Chiba University, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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