SEPARATION OF DIPHTHERIA TOXIN PROTEINS BY SEPHADEX GEL

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Abstract
Diphtheria toxin was separated on Sephadex G-100 into a slowly flocculating fraction of high molecular weight and a rapidly flocculating fraction of low molecular weight associated with the actual toxin. When detoxified, the fraction of low molecular weight forms the protective antigen, but part of this fraction polymerizes to a larger highly protective antigen molecule which can be separated from the slowly flocculating fraction on Sephadex G-200. The rapidly and slowly flocculating fractions were shown to contain distinctly different antigens with separate antibodies. A purification step based on these observations is proposed.