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- W4238275688 abstract "A recombinant HC fragment of botulinum neurotoxin, serotype A (rBoNTA(HC)), has been successfully expressed in a Mut+ strain of the methylotrophic yeast Pichia pastoris for use as an antigen in a proposed human vaccine. Fermentation employed glycerol batch, glycerol-fed batch, and methanol-fed batch phases to achieve high cell density. Induction times were short to maximize rBoNTA(HC) production while minimizing proteolytic degradation. Concentration of rBoNTA(HC) in yeast cell lysates was generally 1–2% of the total protein based on ELISA analysis. The HC fragment was purified from cell lysates using a multistep ion-exchange (IEC) chromatographic process, including SP, Q, and HS resins. The zwitterionic detergent Chaps was included in the buffer system to combat possible interactions, such as protein–protein or protein–DNA interactions. Following IEC was a hydrophobic interaction chromatography (HIC) polishing step, using phenyl resin. The HC fragment was purified to >95% purity with yields up to 450 mg/kg cells based on ELISA and Bradford protein assay. The purified HC fragment of serotype A was stable, elicited an immune response in mice, and was protected upon challenge with native botulinum type A neurotoxin." @default.
- W4238275688 created "2022-05-12" @default.
- W4238275688 date "1998-08-01" @default.
- W4238275688 modified "2023-10-14" @default.
- W4238275688 title "Author Index for Volume 13" @default.
- W4238275688 doi "https://doi.org/10.1006/prep.1998.0948" @default.
- W4238275688 hasPublicationYear "1998" @default.
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