Bouvet J P, Pires R, Pillot J
J Immunol Methods. 1984 Feb 10;66(2):299-305. doi: 10.1016/0022-1759(84)90341-7.
The vast majority of monoclonal IgM proteins is eluted just before the total volume of the column when filtered through G200 Sephadex or S200 Sephacryl gels equilibrated in a 0.005 M phosphate buffer but eluted with 0.05 M phosphate buffer containing 1.7 M NaCl. This unusual behaviour in low-ionic buffer is probably due to the poor solubility of IgM in diluted buffers. It allows a 1-step purification procedure under mild conditions and is suitable for both large and small scale preparations.
当通过在0.005M磷酸盐缓冲液中平衡的G200葡聚糖凝胶或S200琼脂糖凝胶过滤时,绝大多数单克隆IgM蛋白在柱总体积之前被洗脱,但用含有1.7M NaCl的0.05M磷酸盐缓冲液洗脱。在低离子缓冲液中的这种异常行为可能是由于IgM在稀释缓冲液中的溶解度较差。它允许在温和条件下进行一步纯化程序,适用于大规模和小规模制备。