Journal of Experimental Medicine, Vol 142, 664-672, Copyright © 1975 by Rockefeller University Press
Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure
JD Capra, ES Vitetta and J Klein
The murine Ss protein has been isolated and purified. Using specific
antisera, the radiolabeled protein has a mol wt of 120,000 in sodium
dodecyl sulfate polyacrylamide gels. It is composed of two basic subunits
of 23,000 and 14,000 daltons. The smaller molecular weight subunit contains
a single disulfide bridge, is devoid of carbohydrate, and may represent the
murine equivalent of beta2-microglobulin.