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• W1977188081 abstract "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‐β‐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." @default.
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• W1977188081 date "1999-02-05" @default.
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• W1977188081 title "Localization of neutral N-linked carbohydrate chains in pig zona pellucida glycoprotein ZPC" @default.
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• W1977188081 doi "https://doi.org/10.1046/j.1432-1327.1999.00095.x" @default.
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