The Journal of Experimental Medicine
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The Journal of Experimental Medicine, Vol 115, 641-653, Copyright, 1962, by The Rockefeller Institute

ARTICLE

ENZYMATICALLY PRODUCED SUBUNITS OF PROTEINS FORMED BY PLASMA CELLS IN MICE : II. ßbeta;2A-MYELOMA PROTEIN AND BENCE JONES PROTEIN



Brigitte A. Askonas Ph.D.1 and J. L. Fahey M.D.1

1 From the Division of Immunology, National Institute for Medical Research, Mill Hill, London, and the Metabolism Service, National Cancer Institute, National Institutes of Health, Bethesda

The relationship of Bence Jones protein (mol wt = 45,000) to a ß2A-myeloma protein (mol wt = 160,000) formed by the same mouse plasma cell tumor (MPC-2) was investigated. The ß2A-myeloma protein was split by treatment with papain and cysteine into fragments (S20,w = 3.7S), similar in size to the Bence Jones protein (S20,w = 3.6S). Two types of fragments with distinct antigenic groupings designated S and F, were present in the MPC-2 myeloma protein digest. These were partially separated by DEAE-cellulose chromatography.

The Bence Jones protein was found to share antigenic determinants with S fragments from the MPC-2 ß2A-myeloma protein and with S fragments from gamma-globulins. Physicochemical observations indicated, however, that the Bence Jones protein was not identical to the globulin fragments produced by treatment with papain and cysteine.

Comparison of the S and F fragments from ß2A- and gamma-globulins revealed that the antigenic features shared by the various globulins derived from plasma cells (gamma- and ß2A-myeloma proteins, the range of normal gamma-globulins) are largely properties of the S fragments, whereas the distinctive antigenic differences between the gamma- and ß2A-myeloma proteins were properties which appeared in the F fragments of the molecules.

 Submitted on October 16, 1961


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