IO 



Rostoski found that the method of "precipitin" detection 

 fails to distinguish the Bence Jones protein from various pro- 

 teins of human origin. 



III. PROTEOSURIA AND THE BENCE JONES 



PROTEIN. 



Proteoses have been found in the urine in many conditions, 

 usually in minute quantities and as temporary constituents 

 of the urine during the course of specific fevers, inflammatory 

 processes and other diseases. The urinary proteoses present 

 different characteristics from those of the Bence Jones protein, 

 however, and must be sharply distinguished from the latter. 

 Among the most prominent of these differences between the 

 Bence Jones protein and the ordinary proteoses, the following 

 may be indicated in terms of the Bence Jones protein: 



1. Soluble in water (different from heteroproteose). 



2. Coagulated at low temperatures (unlike other proteoses 

 collectively), though elastoses are precipitated by heating their 

 aqueous solutions but redissolve as the temperature falls. 



3. Convertible into acid and alkali albuminates (unlike other 

 proteoses collectively). 



4. Digested by pepsin-HCl, yields primary proteoses except 

 heteroproteose (unlike protoproteose). 



5. Not acted upon by erepsin (different from the primary 

 proteoses). 



6. Excreted in larger quantities than the proteoses. 



7. Does not dialyze through parchment membrane (different 

 from all soluble proteoses). 



8. Not precipitated from a saline solution on dialysis (dif- 

 ferent from many proteoses) . 



9. It is crystallizable (different from all proteoses). 



IV. THEORIES AS TO THE FORMATION OR NATURE 



OF THE BENCE JONES PROTEIN. 

 Kuhne believed the Bence Jones protein to be closely re- 

 lated to heteroproteose on account of the fact that the pure 

 substance, after its precipitation from its solution by heating, 

 is redissolved on further raising the temperature. Huppert 



