Papsidero L D, Johnson E A
Int J Cancer. 1986 May 15;37(5):697-703. doi: 10.1002/ijc.2910370510.
Ductal carcinoma antigen (DCA), as recognized by monoclonal antibody (MAb) F36/22, was purified in high yield and to homogeneity from malignant effusions by means of physicochemical techniques. Fractionation procedures were monitored by immunoenzymometric assays. Preparations purified over 2,000-fold were obtained through acid-extraction, lectin-chromatographies and gel filtration steps. Purified antigen demonstrated a single component upon electrophoretic examination. This material had a high molecular weight and high immunoreactivity. Neuraminidase treatments failed to perturb the antigenicity of the component, indicating an absence of sialic acid residues at the antibody-combining site. Further, extensive proteolytic digestion effected the release of heterogeneous glycopeptides which retained immunologic activity, suggesting the presence of carbohydrate at the active site. Immunologically, DCA was compared with other tumor-associated mucin-like glycoproteins which have been detected in the circulation of patients. Results indicated no cross-reactivity between DCA and other mucins, including CA19-9 and CA-125. Further, no antigenic relationship was noted for purified carcinoembryonic antigen (CEA), also a heavily-glycosylated structure. These data thus suggest that immunological monitoring of disease may be approached using a selected panel of antigenically distinct reagents.
通过物理化学技术，从恶性积液中以高产量和高纯度纯化了导管癌抗原（DCA），该抗原可被单克隆抗体（MAb）F36/22识别。分级分离程序通过免疫酶测定法进行监测。通过酸提取、凝集素色谱和凝胶过滤步骤获得了纯化超过2000倍的制剂。纯化后的抗原在电泳检查时显示为单一成分。该物质具有高分子量和高免疫反应性。神经氨酸酶处理未能干扰该成分的抗原性，表明在抗体结合位点不存在唾液酸残基。此外，广泛的蛋白水解消化导致释放出具有免疫活性的异质糖肽，这表明活性位点存在碳水化合物。在免疫学上，将DCA与在患者循环中检测到的其他肿瘤相关粘蛋白样糖蛋白进行了比较。结果表明DCA与其他粘蛋白（包括CA19-9和CA-125）之间没有交叉反应。此外，对于同样是高度糖基化结构的纯化癌胚抗原（CEA），未发现抗原关系。因此，这些数据表明，可以使用一组抗原性不同的选定试剂来进行疾病的免疫监测。
