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通过与含碳水化合物的聚酰胺胺树枝状大分子形成复合物评估小鼠RegIV/GST融合蛋白的甘露寡糖结合能力。

Manno-oligosaccharide-binding ability of mouse RegIV/GST-fusion protein evaluated by complex formation with the carbohydrate-containing polyamidoamine dendrimer.

作者信息

Kato Yuta, Kochi Kazunori, Unno Hideaki, Goda Shuichiro, Hatakeyama Tomomitsu

机构信息

a Biomolecular Chemistry Laboratory, Graduate School of Engineering , Nagasaki University , Nagasaki , Japan.

出版信息

Biosci Biotechnol Biochem. 2014;78(11):1906-9. doi: 10.1080/09168451.2014.940834. Epub 2014 Jul 29.

Abstract

The carbohydrate-binding properties of the C-type lectin-like mouse RegIV and glutathione S-transferase-fusion protein (GST-mRegIV) were examined using carbohydrate-containing polyamidoamine dendrimers (PD). GST-mRegIV showed affinity for mannan- and manno-oligosaccharide containing PD. Binding was inhibited by manno-oligosaccharides but not by mannose or other tested carbohydrates, suggesting that the binding site may have an extended structure in contrast with typical C-type lectins.

摘要

利用含碳水化合物的聚酰胺胺树枝状大分子(PD)检测了C型凝集素样小鼠RegIV和谷胱甘肽S-转移酶融合蛋白(GST-mRegIV)的碳水化合物结合特性。GST-mRegIV对含甘露聚糖和甘露寡糖的PD表现出亲和力。结合被甘露寡糖抑制,但不被甘露糖或其他测试碳水化合物抑制,这表明与典型的C型凝集素相比,结合位点可能具有延伸结构。

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