122 IMMUNO-CATALYSIS 



8. Anti-Antibodies 



According to the theories of Breinl and Haurowitz, Mudd, Pauhng, 

 and Alexander, etc., the antigens modify the configuration of the 

 normal globulins during their synthesis, resulting in the formation of 

 specific antibody globulins. The antigens exercise this influence to 

 this extent and apparently not further. The statements by Breinl and 

 Haurowitz to the effect that "the orientation of amino acids in the 

 formation of antibodies . . . "; and the "coupling of amino acids to 

 the 'peptide occurs in an orienting environm-ent, namely, the antigen- 

 protoplasm interface." (Mudd), need not therefore be interpreted to 

 imply that amino acids in an antibody molecule occupy diff^erent 

 positions in the peptide chain than those of normal globulins. It may 

 simply mean, as stated by Mudd, that "the chemical groupings coupled 

 to the molecule undergoing synthesis at the antigen surface must he 

 adapted spatially." 



The studies and conclusions of Landsteiner and van der Scheer 

 (1928) were instrumental in the formulation of the above concept. 

 They demonstrated that the steric configuration of antigens exercise 

 distinctive influence on the serological specificity of the antibodies 

 against them; 1- and d-antigenic isomers react specifically with the 

 respective antibodies. These findings brought definite proof for the view 

 that the steric configuration of the antigenic groups is one of the 

 factors determining serological specificity. The mere difference in the 

 position of H, OH and COOH in 1- and d-antigenic isomers sufficed 

 to alter the specificity of the antibody. They also suggested that the 

 steric configuration may play a significant part in the serological spec- 

 ificity of carbohydrates such as those discovered in bacterial anti- 

 gens. This view has been amply confirmed by the extensive studies of 

 Avery and Goebel, et al. Since this subject will be discussed in a latter 

 part of this study, it suffices here to mention that the antibody against 

 galacto-albumin reacted with solutions of galacto-globulin and galac- 

 to-albumin. These antibodies, however, failed to precipitate gluco- 

 albumin. The antibody produced against the antigen containing 

 a-glucoside reacted selectively with this antigen, and not with the 

 antigen containing a /3-glucoside group, and vice versa. A difference in 

 the spatial arrangement of the same polar group therefore exercised 



