动物细胞内 L 型凝集素的重组表达与纯化。
Recombinant Expression and Purification of Animal Intracellular L-Type Lectins.
机构信息
Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Japan.
Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Japan.
出版信息
Methods Mol Biol. 2020;2132:21-28. doi: 10.1007/978-1-0716-0430-4_3.
Animal leguminous-type (L-type) lectins, including ERGIC-53 and VIP36 are responsible for intracellular transport and quality control of N-linked glycoproteins in the early secretory pathway. These lectins possess the carbohydrate recognition domain (CRD), which recognizes high-mannose-type glycans in a Ca-dependent manner. Here we describe the procedures involved in bacterial overproduction and purification of the CRDs of the animal L-type lectins.
动物豆科型 (L 型) 凝集素，包括 ERGIC-53 和 VIP36，负责在早期分泌途径中对 N-连接糖蛋白进行细胞内运输和质量控制。这些凝集素具有碳水化合物识别结构域 (CRD)，以 Ca 依赖性方式识别高甘露糖型聚糖。在这里，我们描述了细菌过量生产和纯化动物 L 型凝集素的 CRD 所涉及的程序。
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