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CHAPTER VI 



SPECIFIC ANTIBODY TO THE B I FUNCTIONAL S- PROTEIN 

 AND TO TWO POST-PREPHENATE PROTEINS 



Specific antibody was made to the purified bifunctional 

 SP-I, to purified arogenate dehydratase and to purified 

 prephenate aminotransferase. SP-I specific antibody was 

 characterized with respect to both SP-I and SP-II. 



Results 

 Antibodies made to each protein (SP-I, ADH and PAT) 

 precipitated crude protein preparations or purified antigens 

 on "Ouchterlony" plates. Each enzyme incubated with the 

 appropriate antibody was precipitated and activity was lost. 

 SP-I specific antibody precipitated both SP-I and SP-II 

 antigen on "Ouchterlony" plates at dilutions of antibody up 

 to 32-fold as seen in Fig. 6-1. The precipitant band was 

 more pronounced for the SP-I plate because more highly 

 concentrated protein was available. A saturation curve of 

 inhibition produced by antibody was similar for both SP-I 

 and SP-II when equal activities were established using 

 0.0084 /xg of SP-I and 0.031 /xg of SP-II (between 0.230 and 

 0.267 nmol min", respectively). Increasing amounts of 



