Inhibition of the Precipitin Reaction by Optically Active Haptens and by Derivatives of the Homologous Hapten

Citation

Bryden, John H. (1945) Inhibition of the Precipitin Reaction by Optically Active Haptens and by Derivatives of the Homologous Hapten. Master's thesis, California Institute of Technology. doi:10.7907/qq08-w397. https://resolver.caltech.edu/CaltechTHESIS:03272025-212241957

Abstract

The work described in this thesis is part of a program of investigation of immunological reactions being carried out at the California Institute of Technology by Drs. Linus Pauling, David Pressman, Dan H. Campbell, and others. Part I consists largely of the results reported in Paper X of the series "The Serological Properties of Simple Substances", published in the Journal of the American Chemical Society.

The phenomenon of hapten inhibition was discovered by Landsteiner, when, to explain the f act that no precipitation occurred with an excess of test azoprotein, he postulated that a reaction did occur between the antibodies and the specific groups of the test antigen, but the products were soluble. A similar effect should be expected if molecules of the simple hapten were present in the solution; i.e., the amount of precipitate formed with optimum amounts of antiserum and antigen should be much less with hapten present than with antiserum and antigen alone. This effect was observed by Landsteiner.

It was also found. that simple compounds having a structure closely similar to that of the homologous hapten would inhibit the precipitation, though to a lesser degree. This fact has been utilized in this investigation as described in Part I, using d- and ℓ-N-(α-methylbenzyl) succinamic acid, a derivative of N-benzylsuccinamic acid which closely resembles the homologous hapten, succinanilic acid. The affect of various substituents in various positions on the molecule of the homologous hapten is described in Part II.

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