Purification of antibodies by immunoadsorbents

The use of immunoadsorbents for the purification of antibodies has been investigated. An immunoadsorbent was prepared by coupling bovine serum albumin (BSA) to ehtylene maleic anhydride copolymer (EMA) at 0C, and used to adsorb rabbit anti-BSA antibodies from an ammonium sulphate precipitated globulin fraction of the antiserum. The antibodies were eluted by a column procedure with phosphate buffered 8 M urea or stepwise with 0.35 M glycine-HCl buffer pH 3.0, 2.5 and 2.0. Using urea to elute and a modification of the original procedure, recovery based on precipitable nitrogen was 42%. Purity was 50% based on the proportion of total nitrogen recovered which was precipitable. The yield was 10% higher than that obtained with the original procedure. When tested with normal rabbit gamma globulin, suggestive evidence was obtained for negligible amounts of non-specific adsorption. A batchwise method of elution was investigated and found to be less efficient than the column procedure