Endoglycosidase and glycoamidase release of N-linked glycans.
Endoglycosidase and glycoamidase release of N-linked glycans.
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DOI：
10.1002/0471142735.im0815s89
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发表时间：
2010-04-01
影响因子：
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通讯作者：
Kranz, Christian
中科院分区：
文献类型：
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作者：
Freeze, Hudson H;Kranz, Christian
几乎所有进入内质网（ER）内腔的蛋白质在进入细胞器、质膜或细胞外间隙的途中都被糖基化。许多聚糖可以连接到蛋白质上，但最常见的是N-连接聚糖（寡糖）。这些链在蛋白质进入ER后很快就被添加，但它们经历了广泛的重塑（加工），特别是在高尔基体中。加工改变了N-聚糖对切割整个糖链或单个单糖的酶的敏感性，这也改变了蛋白质在SDS凝胶上的迁移。这些变化可用于指示蛋白质何时通过特定的亚细胞位置。本单元详细介绍了一些用于跟踪蛋白质的方法，因为它从ER到高尔基体向其最终位置运输。
Nearly all proteins entering the lumen of the endoplasmic reticulum (ER) become glycosylated en route to a cellular organelle, the plasma membrane, or the extracellular space. Many glycans can be attached to proteins, but the most common are the N-linked glycans (oligosaccharides). These chains are added very soon after a protein enters the ER, but they undergo extensive remodeling (processing), especially in the Golgi. Processing changes the sensitivity of the N-glycan to enzymes that cleave entire sugar chains or individual monosaccharides, which also changes the migration of the protein on SDS gels. These changes can be used to indicate when a protein has passed a particular subcellular location. This unit details some of the methods used to track a protein as it trafficks from the ER to the Golgi toward its final location.