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建立了ｐ５３单克隆抗体ｐＡｂ１８０１的免疫亲和层极法纯化ｐ５３蛋白，所纯化的ｐ５３蛋白经ＷｅｓｔｅｒｎＢｌｏｔ（ＥＣＬ法）检测证明：用此法从ｐ５３阳性的ＳＷ４８０细胞中分离到ｐ５３蛋白。银染显示ｐＨ２．０甘氨酸缓冲液比ｐＨ２．８的甘氨酸缓冲液洗脱效果好，这种方法的建立将为分离肿瘤细胞中引起ｐ５３蛋白功能失活和研究肿瘤发生机制提供一种有效途径。
The p53 protein was purified by immunoaffinity-layer method using p53 monoclonal antibody pAb1801. The purified p53 protein was verified by Western Blot (ECL). The p53 protein was isolated from p53-positive SW480 cells by this method. Silver staining showed that pH2.0glycine buffer had a better elution effect than glycine buffer pH2.8. The establishment of this method will provide an effective way to isolate the function of p53 protein in tumor cells and to study the mechanism of tumorigenesis.