Irons L I, MacLennan A P
Biochim Biophys Acta. 1979 Sep 29;580(1):175-85. doi: 10.1016/0005-2795(79)90208-3.
The lymphocytosis promoting factor-haemagglutinin of Bordetella pertussis was isolated from solutions obtained after cell disintegration by a novel affinity chromatographic method using an adsorbent composed of human haptoglobin covalently attached to a Sepharose 4B matrix. The haemagglutinin was bound to the adsorbent at pH 6.5 and eluted by a stepwise change to a pH 10 buffer. A 300--600-fold purification of the haemagglutinin was achieved by this one-step process. The chemical and biological properties of the haemagglutinin isolated by affinity chromatography were found to be similar to those of the protein isolated by other workers from culture supernatants. The affinity chromatographic method was found to be specific for the purification of the lymphocytosis promoting factor-haemagglutinin and no purification of the fimbrial-haemagglutinin of Bordetella pertussis was achieved by the method.
百日咳博德特氏菌的淋巴细胞增多促进因子-血凝素，是通过一种新型亲和色谱法从细胞裂解后获得的溶液中分离出来的。该方法使用的吸附剂是由与人触珠蛋白共价连接到琼脂糖4B基质上组成的。血凝素在pH 6.5时与吸附剂结合，并通过逐步改变为pH 10的缓冲液进行洗脱。通过这一步骤，血凝素实现了300至600倍的纯化。通过亲和色谱法分离得到的血凝素的化学和生物学特性，被发现与其他研究人员从培养上清液中分离得到的蛋白质相似。亲和色谱法被发现对纯化淋巴细胞增多促进因子-血凝素具有特异性，该方法未实现百日咳博德特氏菌菌毛血凝素的纯化。
