Kaetzel C S, Mather I H, Bruder G, Madara P J
Biochem J. 1984 May 1;219(3):917-25. doi: 10.1042/bj2190917.
The isolation of a hybridoma cell line, C-41, secreting monoclonal antibody to bovine xanthine oxidase (EC 1.2.3.2), is described. The specificity of this antibody was determined by solid-phase immunoassay, immunoblotting procedures, affinity chromatography, immunoelectrophoresis and precipitation techniques. The results are compared with those obtained in similar specificity studies on a previously described monoclonal antibody secreted by hybridoma cell line A-94 [Mather, Nace, Johnson & Goldsby (1980) Biochem. J. 188, 925-928]. This latter antibody appears to bind to xanthine oxidase only when the enzyme is immobilized on a solid support such as a plastic plate or nitrocellulose paper. Potential problems in the determination of the specificity of monoclonal antibodies, especially towards membrane proteins of unknown biological activity, are discussed.
本文描述了一种杂交瘤细胞系C-41的分离，该细胞系分泌抗牛黄嘌呤氧化酶（EC 1.2.3.2）的单克隆抗体。通过固相免疫测定、免疫印迹法、亲和层析、免疫电泳和沉淀技术确定了该抗体的特异性。将这些结果与之前由杂交瘤细胞系A-94分泌的单克隆抗体进行类似特异性研究所得结果进行了比较[马瑟、纳斯、约翰逊和戈德斯比（1980年）《生物化学杂志》188卷，925 - 928页]。后一种抗体似乎仅在酶固定于塑料板或硝酸纤维素纸等固相支持物上时才与黄嘌呤氧化酶结合。讨论了测定单克隆抗体特异性时的潜在问题，尤其是针对具有未知生物活性的膜蛋白的特异性测定问题。
