Soluble proteins of human bronchogenic carcinomas.
Solid-phase affinity chromatography has been used to search for tumor-associated proteins of bronchogenic carcinomas. All of the apparently normal proteins were removed from extracts of squamous cell carcinoma, large cell carcinoma, and adenocarcinoma of the lung. The remaining soluble proteins were partially characterized as to heat stability, approximate molecular size, electrophoretic mobility, and biologic function. These tumor-associated proteins were not tumor-specific by current definition. Neither lung cancer patients' lymphocytes nor serum proteins were specifically reactive with these tumor-associated proteins.
D000230:Adenocarcinoma / Q000032:analysis / Q000276:immunology; D000951:Antigens, Neoplasm / Q000032:analysis; D002277:Carcinoma / Q000032:analysis / Q000276:immunology; D002283:Carcinoma, Bronchogenic / Q000032:analysis* / Q000276:immunology; D002294:Carcinoma, Squamous Cell / Q000032:analysis / Q000276:immunology; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007122:Immunoelectrophoresis; D008175:Lung Neoplasms / Q000032:analysis* / Q000276:immunology; D009363:Neoplasm Proteins / Q000032:analysis*; D012995:Solubility
D000951:Antigens, Neoplasm; D009363:Neoplasm Proteins