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Production of recombinant botulinum protein vaccine candidate reported.
2003 OCT 1 - (NewsRx.com & NewsRx.net) -- Researchers have produced a recombinant protein vaccine candidate using the botulinum neurotoxin heavy chain fragment.
"Structural conversion of the serotype A recombinant botulinum neurotoxin heavy chain fragment (rBoNTA(H[subscript]c) produced intracellularly in Pichia pastoris yeast was observed and characterized during purification development efforts," scientists writing in the Journal of Biotechnology report.
"A pH screening study captured the transformation stages of the original recovered species into its derived counterpart and a number of analytical tools such as peptide mapping by LC/MS confirmed the formation of a disulfide bond, especially in samples of neutral to basic pH," stated Anne Bouvier and collaborators at Diosynth RTP Inc. and DynPort Vaccine Company, LLC in the United States. "A cation exchange chromatographic method proved useful in following the incidence of the reaction in various rBoNTA(H[subscript]c) samples. The disulfide formation kinetics were characterized using a one-quarter quadratic factorial design, following the investigation and development of controlled oxidation conditions using cysteine and cystamine as the redox pair"
"Temperature, pH, and concentration of the redox pair had a significant effect on the ...
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Source: HighBeam Research, Production of recombinant botulinum protein vaccine candidate...