一种用于检测墨西哥皱果苋凝集素与糖蛋白结合的表面等离子体共振分析方法。

A surface plasmon resonance assay for the binding of Amaranthus hypochondriacus var. Mexico lectin to glycoprotein.

作者信息

Ozeki M, Furuichi Y, Umekawa H, Takahashi T

机构信息

Department of Agricultural Chemistry, Faculty of Bioresources, Mie University, Japan.

出版信息

Biochem Mol Biol Int. 1998 Jan;44(1):211-6. doi: 10.1080/15216549800201232.

DOI:10.1080/15216549800201232

PMID:9503165

Abstract

We have used the analytical system based on surface plasmon resonance to monitor the interaction between Amaranthus hypochondriacus var. Mexico lectin and four different fetuins; fetuin, asialofetuin, agalactofetuin, and agalactosaminofetuin. Agalactofetuin and agalactosaminofetuin were prepared by enzymic digestion of asialofetuin using jack bean beta-galactosidase or endo-alpha-N-acetylgalactosaminidase from Diplococcus pneumoniae. Ligands were immobilized onto a sensor surface via amide linkages. The lectin interacted most strongly with asialofetuin, but not with agalactosaminofetuin. The binding of the lectin to asialofetuin was inhibited by N-acetylgalactosamine or Gal beta 1-->3GalNAc in a dose-dependent manner.

摘要

我们使用了基于表面等离子体共振的分析系统来监测墨西哥苋凝集素与四种不同胎球蛋白之间的相互作用；胎球蛋白、去唾液酸胎球蛋白、无半乳糖胎球蛋白和无半乳糖胺胎球蛋白。无半乳糖胎球蛋白和无半乳糖胺胎球蛋白是通过用刀豆β-半乳糖苷酶或肺炎双球菌的内切α-N-乙酰半乳糖胺酶对去唾液酸胎球蛋白进行酶消化制备的。配体通过酰胺键固定在传感器表面。凝集素与去唾液酸胎球蛋白的相互作用最强，但与无半乳糖胺胎球蛋白没有相互作用。凝集素与去唾液酸胎球蛋白的结合受到N-乙酰半乳糖胺或Galβ1→3GalNAc的剂量依赖性抑制。