422 BACTERIOLOGICAL CHEMISTRY 



in a pattern complementary to that of the particular 

 part of the antigen in contact with them. The newly 

 synthesised modified globulin chain becomes released 

 from the cells as illustrated by (iii), and ultimately one 

 end of the chain becomes dissociated from the antigen as 

 at (iv), and the central part of the chain can then take 

 up its normal globulin folding (v). In time the other 

 end of the molecule is dissociated from the antigen and 



B 



111 



c Antibodu 



B,.-— ^ R B \ 



G"# 



(ivj (v) (vi) 



Fig. 9 — Synthesis of Antibod}^ Globulin. 



the complete antibody globulin molecule is set free (vi) 

 into the blood-stream, leaving the antigen molecule 

 available to influence the folding of the ends of the peptide 

 chains of freshly formed globulin molecules. The rate 

 of antibody synthesis will depend on the strength of the 

 attraction between the coiled ends of the globulin chain 

 and the determinant groups on the antigen ; the weaker 

 the determinant groups the less time will occur before the 

 attraction is overcome in the ordinary dynamic inter- 

 change which is constantly going on between molecules. 

 Antil^ody molecules Avill continue to be produced until 

 their concentration becomes so great that the antigen 



