期刊
GLYCOCONJUGATE JOURNAL
卷 17, 期 10, 页码 705-711出版社
SPRINGER
DOI: 10.1023/A:1011022721545
关键词
lectin specificity; sialic acids; haemagglutination inhibition; ovine placenta
The specificity of the sialic acid-binding lectin from ovine placenta was examined in detail by haemagglutination inhibition assays applying a panel of 32 synthetic sialic acid analogues. The carboxylic acid group is a prerequisite for the interaction with the lectin, the alpha -anomer of the methyl glycoside is only a little more effective as an inhibitor than the beta -anomer and the most potent inhibitor was 9-deoxy-10-carboxylic acid Neu5Ac, followed by 4-oxo-Neu5Ac. In contrast to the majority of known sialic acid-binding lectins, the N-acetyl group of Neu5Ac is not indispensable for binding, neither is the hydroxyl group at C-9 since substitutions at this carbon atom are well tolerated. Furthermore, all sulfur-containing substituents at C-9 enhanced the affinity of the lectin. This is the first sialic acid-binding lectin found to strongly bind thio derivatives.
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