Purification of anthrax-toxin components by high-performance anion-exchange, gel-filtration and hydrophobic-interaction chromatography

Biochem J. 1988 Jun 15;252(3):753-8. doi: 10.1042/bj2520753.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anthrax / metabolism*
  • Antigens, Bacterial*
  • Bacterial Toxins / isolation & purification*
  • Bacterial Toxins / toxicity
  • Chromatography, Affinity
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Electrophoresis, Polyacrylamide Gel
  • Immunodiffusion
  • Mice

Substances

  • Antigens, Bacterial
  • Bacterial Toxins
  • anthrax toxin