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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Site-specific de-N-glycosylation of diglycosylated ovalbumin in hen oviduct by endogenous peptide: N-glycanase as a quality control system for newly synthesized proteins
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Site-specific de-N-glycosylation of diglycosylated ovalbumin in hen oviduct by endogenous peptide: N-glycanase as a quality control system for newly synthesized proteins

机译:内源性肽对雌性输卵管中二糖基化卵清蛋白的位点特异性N-糖基化:N-聚糖酶作为新合成蛋白质的质量控制体系

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摘要

Hen ovalbumin (OVA) is known to exist as a singly N-glycosylated form with a glycan chain on Asn-292 in egg white. Previous studies showed that di-N-glycosylated form of OVA [Di-OVA; CHO-Asn-292/CHO-Asn-311 (CHO, N-glycan chain)], which has two N-glycan chains on Asn-292 and Asn-311, was expressed only transiently in hen oviduct. Di-OVA was not found in egg white, suggesting that this form cannot be secreted normally and may possibly be converted to mono-N-glycosylated OVA (CHO-Asn-292/Asp-311) by the action of peptide:N- glycanase (PNGase) during synthesis and secretion.
机译:已知卵清蛋白(OVA)以N-糖基化形式存在,在蛋清中的Asn-292上具有聚糖链。先前的研究表明OVA的二-N-糖基化形式[Di-OVA; CHO-Asn-292 / CHO-Asn-311(CHO,N-聚糖链)]在鸡的输卵管中仅瞬时表达,在Asn-292和Asn-311上有两条N-聚糖链。在蛋清中未发现Di-OVA,这表明该形式不能正常分泌,可能通过肽:N-聚糖酶的作用转化为单N-糖基化的OVA(CHO-Asn-292 / Asp-311) (PNGase)在合成和分泌过程中。

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