Guhathakurta B, Sasmal D, Ghosh A N, Pal C R, Datta A
Division of Biochemistry, National Institute of Cholera and Enteric Diseases, Calcutta, India.
FEMS Immunol Med Microbiol. 1996 Jun;14(2-3):63-6. doi: 10.1111/j.1574-695X.1996.tb00271.x.
A cell-associated hemagglutinin (HA) was isolated and purified from a clinical isolate of Shigella dysenteriae type 1 by affinity chromatography on a fetuin-agarose column. The purified hemagglutinin produced a single-stained protein band of around 66 kDa in sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). In an immunodiffusion test, HA-antisera produced a single precipitin band against the purified HA without exhibiting any reactivity towards lipopolysaccharide (LPS) of S. dysenteriae type 1 strain. Inhibition of the hemagglutination by the glycoproteins fetuin, asialofetuin and a sugar derivative N-acetyl-neuraminic acid but not by simple sugars, suggested the specific requirement of complex carbohydrate for binding. Electron micrographs of the purified HA revealed a morphology typical of globular protein.
通过在胎球蛋白-琼脂糖柱上进行亲和层析，从一株1型痢疾志贺氏菌临床分离株中分离并纯化出一种细胞相关血凝素（HA）。在十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）中，纯化的血凝素产生了一条约66 kDa的单染色蛋白带。在免疫扩散试验中，HA抗血清针对纯化的HA产生了一条单一沉淀带，而对1型痢疾志贺氏菌菌株的脂多糖（LPS）没有任何反应。糖蛋白胎球蛋白、去唾液酸胎球蛋白和糖衍生物N-乙酰神经氨酸可抑制血凝，而单糖则不能，这表明结合需要复杂碳水化合物。纯化HA的电子显微镜照片显示出典型的球状蛋白形态。
