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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%.