Assessment of weak sugar-binding ability using lectin tetramer and membrane-based glycans
Assessment of weak sugar-binding ability using lectin tetramer and membrane-based glycans
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使用凝集素四聚体和膜聚糖评估弱糖结合能力
DOI：
10.1007/978-1-4939-1292-6_36
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
K.
中科院分区：
文献类型：
--
作者：
Yamamoto;K.
为了考虑蛋白质糖基化的生物学意义，有必要评估凝集素介导的糖识别过程的重要性。虽然糖和蛋白质，特别是动物凝集素之间的相互作用非常弱，Kd约为10− 4 M，但通过糖-蛋白质相互作用介导的细胞和分子排斥通过细胞表面上的受体及其配体的自缔合使其亲合力增加1-3个数量级。为了评估凝集素和它们的糖配体之间的弱相互作用，我们使用流式细胞术建立了凝集素四聚体与细胞表面聚糖的结合。该策略是高度敏感的，并且可用于确定推定的凝集素结构域是否可能具有糖结合能力。
To consider biological significance of glycosylation of proteins, it is necessary to evaluate the importance of sugar-recognition processes mediated by lectins. Though the interaction between sugars and proteins, especially animal lectins, is quite weak withKdapproximately 10−4M, cellular and molecular recognitions mediated via sugar–protein interaction increase their avidity by 1–3 orders of magnitude by the self-association of both receptors and their ligands on cell surfaces. To assess the weak interaction between lectins and their sugar ligands, we established lectin tetramer binding to cell surface glycans using flow cytometry. This strategy is highly sensitive, and useful to determine whether or not a putative lectin domain may have sugar-binding ability.