An electrophoretic study of the mechanism of precipitin reactions.

  • 1 January 1958
    • journal article
    • Vol. 1  (1) , 36-45
Abstract
The compounds formed by tobacco mosaic virus and by human serum albumin with their antibodies were studied electrophoretically. Those formed by the virus at different antigen/antibody ratios in the reacting mixtures differed greatly in their electrophoretic mobility which ranged from the mobility of free antigen to the mobility approaching that of free antibody. The differences in the mobility probably resulted from corresponding differences in antigen/antibody ratios in the antigen-antibody compounds. By contrast, human serum albumin formed compounds of a constant, or nearly constant, mobility irrespective of antigen/antibody ratios in the reacting mixtures, and when the precipitate formed at equivalence was dissolved in a solution of antigen, the amount of free antigen separated from the compound by electrophoresis was apparently the same as that in which the precipitate was dissolved. This and other evidence suggests that the albumin combined with its antibody at a constant ratio to form a compound that was stable during electrophoresis. The ratio was that of equivalence. More antigen combined with antibody when the antigen was in excess, so that a soluble compound was formed, but then the combination was so loose that the compound dissociated during electrophoresis. The compound with the equivalence ratio was reconstituted and separated from free antigen by electrophoresis. It precipitated in the electrophoretic cell.

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