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Abstract
We report the use of pressures ranging to 2000 atm to elute bovine serum albumin from a moderate affinity monoclonal antibody immunoadsorbent (K = 2.4 × 107 M−1). Over 75 percent of reversibly bound protein was recovered following a single 15 minute incubation at 2000 atm, and over 90 percent recoveries were obtained by repeated pressurizations. Repeated pressurizations to 2000 atm exerted no detrimental effect on immunoadsorbent binding properties, whereas immunoadsorbent binding capacity was significantly reduced upon treatment with a common chemical eluent, glycine/HCl at pH 2.5.Cite this article
Olson, W., Leung, S. & Yarmush, M. Recovery of Antigens From Immunoadsorbents Using High Pressure. Nat Biotechnol 7, 369–373 (1989). https://doi.org/10.1038/nbt0489-369 