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通过制备嵌合凝集素改变紫羊蹄甲凝集素的碳水化合物结合特异性。

Alteration of the carbohydrate-binding specificity of the Bauhinia purpurea lectin through the preparation of a chimeric lectin.

作者信息

Yamamoto K, Konami Y, Osawa T, Irimura T

机构信息

Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, University of Tokyo.

出版信息

J Biochem. 1992 Jan;111(1):87-90. doi: 10.1093/oxfordjournals.jbchem.a123724.

DOI:10.1093/oxfordjournals.jbchem.a123724
PMID:1607368
Abstract

A chimeric lectin gene was constructed by using a cDNA clone coding the Bauhinia purpurea lectin (BPA) in which a part of the metal-binding region was replaced by the corresponding region of the mannose-binding Lens culinaris lectin (LCA). The chimeric lectin expressed in Escherichia coli was found to bind alpha mannosyl-bovine serum albumin (BSA) and this binding was inhibited by mannose.

摘要

通过使用编码紫羊蹄甲凝集素(BPA)的cDNA克隆构建了一个嵌合凝集素基因,其中金属结合区域的一部分被甘露糖结合的兵豆凝集素(LCA)的相应区域所取代。发现在大肠杆菌中表达的嵌合凝集素能结合α-甘露糖基牛血清白蛋白(BSA),并且这种结合被甘露糖抑制。

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Alteration of the carbohydrate-binding specificity of the Bauhinia purpurea lectin through the preparation of a chimeric lectin.通过制备嵌合凝集素改变紫羊蹄甲凝集素的碳水化合物结合特异性。
J Biochem. 1992 Jan;111(1):87-90. doi: 10.1093/oxfordjournals.jbchem.a123724.
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