A simple novel approach for the purification of pertussis toxin
1988
Mégret, Françoise | Alouf, J. E. (Joseph E.)
Pertussis toxin (PT) was purified from concentrated culture supernatants of Bordetella pertussis by a single step based on affinity chromatography on heparin‐Sepharose 6B with a recovery of 36% in two fractions. The fraction of highest specific activity (0.91 mg of toxin per mg protein) constituted 15.3% of toxin content in crude material and appeared homogeneous by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. It exhibited the five bands corresponding to toxin subunits. The purified fraction induced clustering of Chinese hamster ovary cells at as little as 0.06 ng per ml. PT solution gave a single precipitation line with rabbit immune serum raised against crude Bordetella pertussis supernatant.
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