i66 Bcnce Jones Protein — Multiple Myeloma [Dec. 



seriim globulin. He supposes it is produced by the digestive action 

 of leucocytes or bacteria, or, more particularly, by the enzymotic 

 action of plasma cells in the bone marrow. Moitessier (21) be- 

 lieved that Bence Jones protein is derived from blood proteins 

 linder the influence of new bone growth. Lindeman (49) con- 

 cluded that, while Bence Jones protein cannot be put in any present 

 groiip of proteins, it is nearest in relationships to the triie albumins. 

 Abderhalden (50) stated that, jiidging from its yield of amino 

 acids, Bence Jones protein does not correspond to either of the 

 two serum proteins, but may be considered a tissue albumin, which 

 without being broken down or changed into one of the serum 

 albumins, is transmitted to the blood and is then probably elimi- 

 nated as an albumin foreign to the blood. Schulz (65) suggested 

 that the Bence Jones protein might prove to be related to globin. 



Origin from bone. Donetti (44) 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 (16) 

 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 marrow may give rise to Bence Jones protein. Weber 

 and Hutchinson (22) concluded that Bence Jones protein is formed 

 from granules in the myelomatous cells. Virchow (17) believed 

 the substance resulted from degenerative changes in protein occur- 

 ring in sarcomata. Weber (22) also thought it may be due to an 

 abnormal metabolic or degenerative process in the myelocytes, or 

 in the tumor cells derived from the myelocytes or their predecessors. 

 Von Rustizky (45) likewise considered that the substance is pro- 

 duced in connection with new bone growth. Williams (51) 

 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 glycoproteins are more or less broken up and then ex- 

 creted in different degrees of chemical decomposition according to 

 the stage of the disease. In a recent paper Weber and Ledgingham 

 (46) suggested, from the histological evidence in the case of multi- 

 ple myeloma studied by them, that the cytoplasmic residues of 

 karyolyzed plasma cells may be the source of Bence Jones protein. 



