Biological and biochemical properties of soluble tumor-specific transplantation antigen of a simian virus 40-induced neoplasm.
We have solubilized by limited papain digestion and partially purified the tumor rejection antigen, tumor-specific transplantation antigens (TSTA), from membranes of a simian virus 40-induced sarcoma. Uniform-sized materials with a molecular weight range of 50,000 have retained their tumor rejection activities through the purification procedures. The simian virus 40 TSTA have been separated from H-2 activity by affinity chromatography on concanavalin A columns and no evidence was found for H-2 antigens in the unbound fraction (I) of concanavalin A containing TSTA activity. A reduced yield from the crude soluble fraction was observed with Fraction I of concanavalin A material and this may indeed represent fragmentation of antigen during papain digestion. These results stand in contrast to purification of histocompatibility antigens (H-2alpha) using the same methods and techniques. Low concentrations of simian virus 40 TSTA crude soluble materials were nervertheless biologically active. A concentration as low as 4 mug protein provided 50% tumor rejection and 0.1 mug protein provided lymphocyte stimulation. Both assays reflected specificity of response.
D000818:Animals; D000951:Antigens, Neoplasm; D002462:Cell Membrane / Q000276:immunology; D003429:Cross Reactions; D046508:Culture Techniques; D005260:Female; D006649:Histocompatibility Antigens; D008213:Lymphocyte Activation; D051379:Mice; D008807:Mice, Inbred BALB C; D012513:Sarcoma, Experimental / Q000209:etiology / Q000276:immunology*; D013539:Simian virus 40; D013154:Spleen / Q000166:cytology / Q000276:immunology
D000951:Antigens, Neoplasm; D006649:Histocompatibility Antigens