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Purification of anthrax-toxin components by high-performance anion-exchange, gel-filtration and
C P Quinn1, C C Shone, P C Turnbull
1Public Health Laboratory Service, Centre for Applied Microbiology and Research, Salisbury, Wilts, U.K.
The Biochemical Journal
|June 15, 1988
Abstract:
A procedure has been developed for purification of the tripartite anthrax-toxin components. This involves sequential high-performance anion-exchange, gel-filtration and hydrophobic-interaction chromatography. From an initial culture volume of 15 litres, typical yields of 8 mg of protective antigen, 13 mg of lethal factor and 7 mg of oedema factor are produced to higher degrees of purity than have previously been achieved by conventional chromatographic techniques.