Further observations on precipitin reaction of bence-jones protein

Abstract

The studies of the immune reactions of Bence-Jones protein have not given concordant results. The earlier observers (Abderhalden and Rostoski,1 Boggs and Guthrie2) by injecting Bence-Jones proteins in rabbits obtained precipitins that reacted not only with this protein but also with human serum proteins. Massini3 noted a quantitative difference between Bence-Jones protein and blood serum proteins by means of complement fixation. He suggests that Bence-Jones is closely related yet different from the serum proteins, and that the fixation test is not suited for differentiation except with pure preparations. Micheli 4 studied a Bence-Jones protein in the urine, blood, and serous fluids of a patient with lymphosarcoma of the large intestine. Anaphylactic experiments and fixation tests with what he calls strictly pure BenceJones protein, as determined by careful chemical tests, and with human serum gave inter-reactions which Micheli explains as due to the presence in the Bence-Jones protein of two principal receptors, one with the same antigenic properties as the proteins in normal serum; the second, more abundant, being the specific Bence-Jones antigen. In the serum of rabbits injected with urine from cases of myeloma, Hektoen 5 demonstrated specific precipitin reacting with urine or serum containing Bence-Jones protein, but not with normal human serum. Bayne-Jones and Wilson6 found that while noncrystallin forms of Bence-Jones protein, isolated from urine by salting-out or other precipitation methods, contained traces of serum proteins, spontaneously crystallizing Bence-Jones protein, betrayed a specific protein, and was not acted on by antiserum to human serum. The claim by Hektoen 5 that Bence-Jones protein is a distinct antigen is based on the results of absorption experiments as illustrated in table 1.