A Human Tumor-Specific Antigen from Lung Cancer : A New Purification Method

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この論文は国立情報学研究所の学術雑誌公開支援事業により電子化されました。A new purification method for tumor-specific antigens is described. The TS-1 antigen was purified with ammonium sulfate and fractionation by column chromatography, Sephadex G 50,G 200 and Con A Sepharose 4B. It was shown using the double immunodiffusion test that the TS-1 and CEA had a common antigenic determinant. The TS-2 antigen, which was purified by a simpler method using proteolysis of Pronase E and fractionation by column chromatography, was also a tumor-specific antigen. Anti-TS-1 serum had crossreactivity with TS-2 antigen, but anti-CEA and anti-NCA had no crossreactivity in double gel diffusion with TS-2 antigen. It was shown using the immunofluorescence test and enzyme-labelled antibody technique that TS-1 and TS-2 antigens localized only on the cancer cell surface. They were not localized on the normal tissue of bronchial epithelium, mucous glands, vascular tissue or alveoli. The sedimentation coefficients of TS-1 and TS-2 antigens, which were measured by boundary ultracentrifugation, were 6.81 and 1.65,respectively. Sugar parts of the TS-1 antigen were composed of fucose, galactose, glucose, N-acetylglucosamine and sialic acid, while those of the TS-2 antigen were composed of fucose, galactose, N-acetylgalactosamine and unknown sugars. The protein parts of the TS-1 and TS-2 antigens accounted for 11.3% and 15.1%, respectively. While TS-1 antigen and CEA showed affinity to Con A, TS-2 antigen did not. These results suggested that TS-1 and TS-2 antigens were cancer specific and that TS-1 antigen was divided by the proteolysis with Pronase E into TS-2 antigen and NCA.
京都大学の論文
1986-08-31

A Human Tumor-Specific Antigen from Lung Cancer : A New Purification Method

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