Specificity of the binding site of the sialic acid-binding lectin from ovine placenta, deduced from interactions with synthetic analogues |
| |
Authors: | M. Fernanda Troncoso M. Mercedes Iglesias Rainer Isecke Carlota Wolfenstein Todel Reinhard Brossmer |
| |
Affiliation: | (1) Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (IQUIFIB) (UBA-CONICET), Junín 956, 1113 Buenos Aires, Argentina;(2) Biochemistry Center, University of Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany |
| |
Abstract: | 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 -anomer of the methyl glycoside is only a little more effective as an inhibitor than the -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. |
| |
Keywords: | lectin specificity sialic acids haemagglutination inhibition ovine placenta |
本文献已被 SpringerLink 等数据库收录! |
|