Abstract
Summary
Concentrated solutions of tetanus toxoid prepared on a peptone-free medium were examined by electrophoresis in a Tiselius apparatus. The concentrate contained three components—A, present in a very small amount, B and C, present in about equal amounts.
The toxoid concentrate was allowed to react with an absorbed tetanus antitoxic pseudoglobulin, the floccules were separated and the supernatant was examined by electrophoresis. The supernatant contained several components, which bore no definite relation to the pattern of the original toxoid concentrate. By far the major part of the protein in the supernatant moved with a lower mobility than either component B or C. The mobility of F which was present in very small amount corresponded to that of B.
The presence of components D and E in the supernatant is ascribed to the nonreacting protein present in the antitoxin. Since all of component C and nearly all of component B was removed by flocculation, this evidence is taken to indicate that there was present in the toxoid concentrate two different toxoid proteins.
Although this work was done with tetanus toxoid and not with the toxin, consideration of the foregoing statements lends support to the views of Smith and Petrie that tetanus toxin (and by analogy tetanus toxoid) is not a homogeneous solution of toxin or toxoid molecules.
We wish to express our gratitude to Dr. Robert C. Warner of the Eastern Regional Laboratory, Philadelphia, Pa., for performing the electrophoretic experiments and for other valuable assistance.
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