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• W2000453384 abstract "Abstract Immunosorbent chromatography employing monoclonal antibodies (MAB) to Bacillus anthracis protective antigen (PA) was used to purify this toxin from crude fermentation supernatant. Anti-PA MAB were coupled via CNBr to Sepharose CL-4B resin. The immunosorbent, 4 mg MAB/ml resin, had the capacity to bind 1 mg PA/ml resin. At this level PA was completely adsorbed from the inoculum and could be eluted in 2 m NaSCN to result in complete recovery of PA based on antigenic activity after consideration of the antigenic degradation of PA by NaSCN. Minor proteins due to PA degradation, as shown by immunoblot, were removed by gel permeation chromatography to provide a homogeneous product. These experiments represent the first report of the purification of PA by immunosorbent chromatography and illustrate that this technique is the only satisfactory way to purify homogenous PA." @default.
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• W2000453384 date "1988-01-01" @default.
• W2000453384 modified "2023-09-27" @default.
• W2000453384 title "Purification of Bacillus anthracis protective antigen by immunosorbent chromatography" @default.
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• W2000453384 doi "https://doi.org/10.1016/0141-0229(88)90092-0" @default.
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