96 II. FUNDAMENTAL STRUCTURE OF RROTOPLASM 



(22). Thus, the solubility of horse serum globulin is not increased by 

 the presence of pseudoglobulin, but increased by the addition of serum 

 albumin (118). This may be interpreted as due to the unfolding of 

 globulin molecules owing to the presence of albumin. In addition to 

 albumin, various amino acids have shown to increase the solubility of 

 euglobulin (119). As is well known, globulin is soluble in the presence 

 of inorganic salts which as just m^entioned have the spreading action. 

 Serum globulin becomes sedimentable as the serum is dialyzed. In a 

 similar way phage particles can be rendered easily precipitable by the 

 dialysis of the culture filtrate. 



The writer found that serum euglobulin, if isolated by our iso- 

 electric precipitation method, exists in forming virus-like particles. Ac- 

 cording to the writer's opinion (22), the polymerization product of this 

 serum euglobulin, if present in the spreading form, can act as com- 

 plement in immunological reactions, but not so in the coagulated, 

 virus-like particles, which the latter can be expanded on the addition 

 of serum protein with an albumin nature termed end-piece or factor 

 C'2, while the coagulated euglobulin particle is named mid-piece or 

 factor C'l, so that on the addition of end-piece to mid-piece, /. e. the 

 coagulated euglobulin particle, the complement activity may arise. 



A well known virus-like factor of pneumococcus capable of trans- 

 mitting the peculiar character of the coccus, from which it was 

 separated, to another strain of coccus is needed for its function a 

 component present in serum or serous fluids, which can be supplied 

 by a fraction of bovine serum albumin (120). 



As detailed already, protoplasm undergoes coagulation into minute 

 particles on the application of stimulus. This coagulation spreads as 

 a chain reaction in the protoplasm, but reversible in so far as the 

 protoplasm remains "alive." The unfolding of such coagulated proto- 

 plasm may be possible, if certain low-molecular substances are present 

 in the cell protoplasm for their unfolding. 



Phage particles can be seen under the microscope by dark-ground 

 illumination. However, if adsorbed onto bacterial surface they would 

 become always invisible (9), probably due to the unfolding of the 

 particles on the cell surface. In order to show the structure acting 

 as the template, viruses should be required to unfold the peptide 

 chains. If the physicochemical effect resulting from the spatial 

 arrangement of polar groups revealed by the unfolding of a virus 

 particle is stronger than that of the protoplasm, the spatial distribu- 

 tion of polar groups in the protoplasm may be changed by both the 

 electrostatic repulsion and attraction so as to correspond to the pat- 

 tern of virus. The change thus induced in the protoplasm structure 

 must be the virus multiplication itself. 



