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小鼠卵透明带糖蛋白ZP3的O-连接寡糖非还原端的半乳糖对于该糖蛋白的精子受体活性至关重要。

Galactose at the nonreducing terminus of O-linked oligosaccharides of mouse egg zona pellucida glycoprotein ZP3 is essential for the glycoprotein's sperm receptor activity.

作者信息

Bleil J D, Wassarman P M

机构信息

Department of Cell and Developmental Biology, Roche Institute of Molecular Biology, Nutley, NJ 07110.

出版信息

Proc Natl Acad Sci U S A. 1988 Sep;85(18):6778-82. doi: 10.1073/pnas.85.18.6778.

Abstract

During fertilization in mice, zona pellucida glycoprotein ZP3 mediates initial sperm-egg interactions by serving as receptor for sperm. Purified egg ZP3, as well as ZP3-derived O-linked oligosaccharides, exhibit sperm receptor activity in vitro. We report that treatment of purified egg ZP3 and ZP3-derived O-linked oligosaccharides with either alpha-galactosidase or galactose oxidase results in loss of sperm receptor activity. In the latter case, sperm receptor activity can be restored to the oxidized glycoprotein and O-linked oligosaccharides by treatment with sodium borohydride. We conclude that galactose, located in alpha-linkage at the nonreducing terminus of O-linked oligosaccharides, is at least one of the sugar determinants on ZP3 responsible for binding of sperm to the zona pellucida.

摘要

在小鼠受精过程中,透明带糖蛋白ZP3作为精子受体介导精子与卵子的初始相互作用。纯化的卵ZP3以及来源于ZP3的O-连接寡糖在体外表现出精子受体活性。我们报道,用α-半乳糖苷酶或半乳糖氧化酶处理纯化的卵ZP3和来源于ZP3的O-连接寡糖会导致精子受体活性丧失。在后一种情况下,用硼氢化钠处理可使氧化的糖蛋白和O-连接寡糖恢复精子受体活性。我们得出结论,位于O-连接寡糖非还原末端α-连接的半乳糖至少是ZP3上负责精子与透明带结合的糖决定簇之一。

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