BENCE-JONES' PROTEIN 489 



Bence-Jones' protein is derived from blood proteins under the influence of 

 the new bone growth. Lindemann concluded that, while Bence-Jones' pro- 

 tein cannot be put in any present group of proteins, it is nearest in relation- 

 ships to the true proteins. Abderhalden stated that, judging from its- 

 yield of amino acids, Benco-Jones' protein does not correspond to either of 

 the two serum proteins, but may be considered a tissue protein, which, 

 without being broken down or changed into one of the serum proteins, 

 is transmitted to the blood and is then probably eliminated as an protein 

 foreign to the blood. Schultz suggested that the .Bence-Jones' protein 

 might prove to be related to globin. 



Origin from Bone. Donetti believes that Bence-Jones' protein results 

 from some loss of function of the bone-marrow, owing to the destruction of 

 the latter. Hopkins and Savory concluded that it is formed by processes 

 that indicate interruptions in the normal autolytic processes in tissues 

 due to toxin from the growth. They also suppose that the loss of some 

 normal function of the bone-mairow may give rise to Bence-Jones' pro- 

 tein. .Weber and Hutchinson concluded that Bence-Jones' protein is 

 formed from granules in the myelomatous cells. Virchow believed the sub- 

 stance resulted from degenerative changes in protein occurring in sarco- 

 mata. Weber also thought it may be due to an abnormal metabolic or de- 

 generative process in the myelocytes, or in the tumor cells derived from 

 the myelocytes or their predecessors. Von Rustizky likewise considered 

 that the substance is produced in connection with new bone growth. Will- 

 iams thought that Bence-Jones' protein may represent modified glycopro- 

 teins from disorganized bones and tendons. He accounts for the variable 

 properties of Bence-Jones' protein products by assuming that the glycopro- 

 teins are more or less broken up and then excreted in different degrees of 

 chemical decomposition according to the stage of the disease. In a recent 

 paper Weber and Ledgingham suggested, from the histological evidence in 

 the case of multiple myeloma studied by them, that the cytoplasmic resi- 

 dues of karyolyzed plasma cells may be the source of Bence-Jones' pro- 

 tein. Abderhalden by means of his "optical method" has found that the 

 serum from a patient excreting the Bence-Jones' protein digested all the 

 organs of the patient, but not those of another individual. The serum also 

 digested the urinary protein and he thinks the positive results are due to 

 the digestion of the Bence-Jones' protein which is infiltrating all the organs. 



Ottenberg and Gies have found that crude elastose, after its subcuta- 

 neous or intraperitoneal injection, can readily be detected in the urine by 

 the heat precipitation test. Since Bence-Jones' protein has various prop- 

 erties in common with elastoses, Ottenberg and Gies suggested that osseoal- 

 bumoid (bone elastin ?) might be the forerunner of Bence-Jones' protein. 



Several years ago, I endeavored to determine whether osseoalbumoid 

 might be so acted upon by the enzymes present in cells of myelomatous 

 growths as to give rise to a substance having the properties of Bence- 



