Abstract
The usefulness of thiophilic adsorption chromatography for the purification of rat IgG2b monoclonal antibodies has been evaluated. This approach has not shown specificity for immunoglobulins; therefore, to minimize potential interferences, the purification was carried out from supernatants of hybridomas grown in serum- and protein-free conditions. The protein purity of the six final antibody preparations assayed was always ≥97%. In addition to the easiness of this procedure, which enables one-step antibody purification, the materials employed are rather inexpensive and milligram amounts of antibody can be recovered from 1 L of supernatant. Overall, the purification of rat IgG2b monoclonals under the conditions reported here offers an advantageous alternative to other more expensive and cumbersome methods. Copyright © 1999 John Wiley & Sons, Ltd.
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