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Laboratory of Cell Biology, National Cancer Institute, Bethesda, Maryland 20014
Tumor-specific transplantation antigen (TSTA) was solubilized from cell membranes of sarcoma Meth-A with nonionic detergent Nonidet P40. Soluble TSTA was partially characterized by chromatographic separation and electrophoresis. The antigen responsible for tumor rejection activity had a molecular weight of approximately 70,000 daltons in the presence of detergent and an electrophoretic mobility of
-globulin. TSTA was well separated from mouse histocompatibility antigen H-2 by lectin affinity chromatography. The antigen purified by a sequence of procedures, including gel filtration, lectin affinity chromatography, column electrophoresis, and rechromatography on agarose, showed only three major bands on polyacrylamide gel electrophoresis. TSTA was specific for sarcoma Meth-A.
1 To whom requests for reprints should be addressed, at Laboratory of Cell Biology, National Cancer Institute, NIH, Bethesda, Md. 20014.
Received 4/11/77. Accepted 6/20/77.
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