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The Isolation and Characterization of Tumor-specific Antigens of Rodent and Human Tumors¹

Montreal General Hospital Research Institute, McGill University, Montreal, Quebec, Canada H3G 1A4

Putative tumor-specific transplantation antigens (TSTA) from both a carcinogen-induced rodent tumor (MC-1) and 2 human tumors were purified. The antigens were solubilized from the tumor cell membranes by limited papain digestion in a manner similar to that described for the isolation of normal histocompatibility antigens. The antitumor immune response of the tumor-bearing host was used to monitor the purification of the putative TSTA in both the rodent and human tumor systems. In the case of the rodent tumor, a major step in the purification of the TSTA involved affinity chromatography on Sepharose beads coupled to autologous antitumor antiserum. A comparable procedure was utilized in the purification of the TSTA from human tumors by using affinity chromatography on anti-human ß₂-microglobulin antiserum coupled to a solid phase. The data obtained indicate that the TSTA of human tumors contains a ß₂-microglobulin chain that is immunochemically identical with, and very similar in size to, that found in normal human histocompatibility antigens. A subunit of similar size was also identified in the carcinogen-induced rodent tumor. These results suggest that the TSTA in both humans and rodents may well be altered histocompatibility antigens.

¹ Presented at the Symposium "Cancer and Chemistry" as part of the Fourth Conference on Embryonic and Fetal Antigens in Cancer, November 2 to 5, 1975, Charleston, S. C. This work was supported in part by the Medical Research Council of Canada and the Cancer Society of Montreal.

² Presenter.