Immunoaffinity isolation of ductal carcinoma antigen using monoclonal antibody F36/22.
Immunoaffinity isolation of ductal carcinoma antigen using monoclonal antibody F36/22.
复制标题
使用单克隆抗体 F36/22 免疫亲和分离导管癌抗原。
DOI：
10.1016/0161-5890(84)90153-6
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发表时间：
1984
影响因子：
3.6
通讯作者：
Chu,TM
中科院分区：
文献类型：
--
作者：
Papsidero,LD;Croghan,GA;Johnson,EA;Chu,TM
F36/22是一种抗人乳腺肿瘤细胞系的单克隆抗体，可识别癌症患者循环中的一种抗原。用McAb亲和层析法从恶性渗出液中纯化抗原，然后用固定化麦胚凝集素吸附-解吸。电泳分析表明，分离到一个单一的高摩尔。wt糖蛋白表现出pH 4.2附近的等离子点和约4.2的密度。1.45 G/ml.虽然与麦胚凝集素高度反应，但与伴刀豆球蛋白A、小扁豆凝集素和花生凝集素的相互作用可以忽略不计或很弱。该抗原是免疫沉淀的，表明多个单克隆抗体结合位点的发生，并耐热和酸处理。蛋白酶或神经氨酸酶处理后抗原性不受干扰，但暴露于碱性条件下时受到影响。这些结果表明，McAb F36/22识别的是高分子量的DNA。wt组分作为粘蛋白样糖蛋白存在于循环中。
Monoclonal antibody (McAb) F36/22, raised against a human breast tumor line, identifies an antigen found in the circulation of cancer patients. Antigen was purified from malignant effusions using McAb-affinity chromatography followed by adsorption-desorption from immobilized wheat germ lectin. Electrophoretic analysis demonstrated the isolation of a single high mol. wt glycoprotein exhibiting an isoionic point near pH 4.2 and a density of approx. 1.45 g/ml. Although highly reactive with wheat germ lectin, a negligible or weak interaction was observed with concanavalin A, lentil lectin and peanut agglutinin. The antigen was immune-precipitable, indicating the occurrence of multiple McAb-binding sites, and was resistant to heat and acid treatments. Antigenicity was not perturbed following protease or neuraminidase treatments, but was affected upon exposure to alkaline conditions. Taken together, these data suggest that McAb F36/22 recognizes a high mol. wt component occurring in circulation as a mucin-like glycoprotein.