使用单克隆抗体通过免疫亲和色谱法纯化蜡样芽孢杆菌产生的一种肠毒素。

Purification of an enterotoxin produced by Bacillus cereus by immunoaffinity chromatography using a monoclonal antibody.

作者信息

Shinagawa K, Takechi T, Matsusaka N, Sugii S

机构信息

Department of Veterinary Medicine, Faculty of Agriculture, Iwate University, Japan.

出版信息

Can J Microbiol. 1992 Feb;38(2):153-6. doi: 10.1139/m92-025.

DOI:10.1139/m92-025

PMID:1521189

Abstract

A murine monoclonal antibody (MAb) with high reactivity to an enterotoxin produced by Bacillus cereus was used to prepare an immunoadsorbent for purification of the enterotoxin. By immunoaffinity chromatography using the immunoadsorbent, approximately 25% of crude enterotoxin applied was recovered in the eluate. The purified enterotoxin was found to be electrophoretically and antigenically homogeneous. It also showed vascular permeability activity and mouse lethality, and caused fluid accumulation in mouse ligated intestinal loops, whereas it did not show any hemolytic and lecithinase activities. Thus, immunoaffinity chromatography proved useful in the purification of enterotoxin produced by B. cereus in terms of recovery, purity, and relative ease of performing the purification.

摘要

一种对蜡样芽孢杆菌产生的肠毒素具有高反应性的鼠单克隆抗体（MAb）被用于制备用于纯化该肠毒素的免疫吸附剂。通过使用该免疫吸附剂进行免疫亲和层析，施加的粗制肠毒素中约25%在洗脱液中回收。纯化后的肠毒素在电泳和抗原性方面均表现出均一性。它还表现出血管通透性活性和小鼠致死性，并导致小鼠结扎肠袢积液，而未表现出任何溶血和卵磷脂酶活性。因此，就回收率、纯度以及进行纯化的相对简易性而言，免疫亲和层析被证明对纯化蜡样芽孢杆菌产生的肠毒素很有用。