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A tumor antigen isolated from the cytosol of a methylcholanthrene-induced sarcoma (Meth A) has been purified to homogeneity by the criteria of two-dimensional gel analysis and NH2- and COOH-terminal sequencing. The purified antigen has a mol. wt of 82,000 by SDS gel electrophoresis. However, the apparent mol. mass of the antigen was found to be 71,600 and 67,700 by gel filtration chromatography and sedimentation analysis, respectively. It is not a glycoprotein, possesses an acidic isoelectric point (6.0) and exists as dimeric and monomeric species. The dimer is not held together by disulfide bonds. The purified protein retains its ability to induce transplantation immunity in syngeneic hosts when challenged with Meth A sarcomas. Chemical analyses of the NH2- and COOH-termini gave the following sequences: NH2-PKPINVRVTTMDAELEFAIQPN and IDE(F,A)EM-COOH, respectively.
S J Ullrich, and
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E Appella
January 1994,
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S J Ullrich, and
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S J Ullrich, and
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S J Ullrich, and
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E Appella
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S J Ullrich, and
E A Robinson, and
E Appella
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S J Ullrich, and
E A Robinson, and
E Appella
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S J Ullrich, and
E A Robinson, and
E Appella
June 1987,
Cancer research,
