44 



II. FUNDAMENTAL STRUCTURE OF PROTOPLASM 



be regarded as the growth of this crystal, wherein each amino acid 

 may be adsorbed to the corresponding site to produce the perfect pro- 

 toplasm proteins as suggested by Haurowitz. Even a complete protein 

 molecule having a configuration slightly different from that of the pro- 

 toplasm protein may sometimes be adsorbed, and after being changed 

 into the configuration same as that of the protoplasm protein by the 

 spatial rearrangement of its polar groups, may be fused into the pro- 

 toplasm as in the manner shown in Fig. 7. 



e-€)— e-^ 



Protein to be 

 assimilized 



© — u — (±> 



e-€)— e-€) 



Protoplasm Q (^ Q Q 



G) — R — ^ 



Fig. 7. Diagrammatic illustration of assimilase action of protoplasm. 



I ; The arrangement of polar groups in the protein to be assimilized 

 is different from that of the protoplasm in the sites shown by arrows. 



II: The protein is fused into the protoplasm following the. rearrange- 

 ment of polar groups. 



In this respect, the writer regards protoplasm as a kind of en- 

 zymes, designated as "assimilase". As will be discussed in the next 

 chapter, the action of this assimilase is considered as arising from the 

 polymerization of the same protein molecules. A powerful physico- 

 chemical force may be generated in the assimilase by the spatial 

 arrangement of polar groups piled up by the polymerization of proteins, 

 a force which can cause the rearrangement of the polar forces in the 

 adsorbed protein. 



