The Journal of Experimental Medicine
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The Journal of Experimental Medicine, Vol 92, 337-347, Copyright, 1950, by The Rockefeller Institute for Medical Research New York

ARTICLE

STUDIES ON PEROXIDATIVE DETOXIFICATION OF PURIFIED DIPHTHERIA TOXIN

Kjell Agner M.D.1

1 From the Department of Microbiology, New York University College of Medicine, New York, and the Laboratory of Physical Chemistry, University of Wisconsin, Madison

The mechanism of the peroxidative oxidation of diphtheria toxin has been investigated. It has been found that this reaction requires the presence of an oxidizable, dialyzable cofactor in addition to hydrogen peroxide and peroxidase. Cofactors are present in a variety of materials and have been partially purified from urine.

The flocculation titer of toxin modified by peroxidation remains unchanged even after 99 per cent or more of the toxicity has been destroyed. The change thus appears analogous to the conversion of toxin to toxoid in the presence of formalin.

It is suggested that the well known conversion of crude diphtheria toxin to toxoid which occurs on storage or aging may be due to a slow peroxidative process.

 Submitted on July 7, 1950


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