Balint J P
IMRE Corporation, Seattle, Washington 98109-4933.
Immunol Invest. 1990 Feb;19(1):81-9. doi: 10.3109/08820139009042027.
Studies were performed to determine if murine monoclonal immunoglobulin G1 (IgG1) could be purified from ascites fluid employing specific immuno-affinity chromatography. Murine polyclonal IgG was first removed from the ascites fluid by passage over immobilized protein A at pH 7.0. Analysis of the ascites fluid after this procedure revealed that murine monoclonal IgG1 did not bind to the protein A under the conditions employed. Additional analyses revealed that murine polyclonal IgG bound to and could be eluted from the immobilized protein A. Subsequent passage of the ascites fluid through an immunoadsorbent containing sheep antibody to murine monoclonal IgG1 revealed that the murine monoclonal IgG1 isotype was specifically removed. Analyses of the immunoglobulin eluted from the immuno-affinity matrix revealed the presence of murine monoclonal IgG1 with purities equal to or greater than 95%.
开展了多项研究，以确定是否可以采用特异性免疫亲和色谱法从腹水液中纯化小鼠单克隆免疫球蛋白G1（IgG1）。首先通过在pH 7.0条件下使腹水液通过固定化蛋白A，去除其中的小鼠多克隆IgG。对该步骤后的腹水液进行分析发现，在所采用的条件下，小鼠单克隆IgG1不与蛋白A结合。进一步分析表明，小鼠多克隆IgG与固定化蛋白A结合并可从其上洗脱下来。随后使腹水液通过含有抗小鼠单克隆IgG1羊抗体的免疫吸附剂，结果显示小鼠单克隆IgG1同型被特异性去除。对从免疫亲和基质上洗脱的免疫球蛋白进行分析，结果显示存在纯度等于或高于95%的小鼠单克隆IgG1。
