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作 者:梁平[1] 韩本立[1] 赵晓晏[1] 于世远[1] 郭萍[1]
机构地区:[1]第三军医大学附属新桥医院肝胆外科 消化内科 附属西南医院肝胆外科中心
出 处:《第三军医大学学报》1996年第4期298-302,共5页Journal of Third Military Medical University
基 金:国家自然科学基金
摘 要:从人胆管癌组织中提纯了一种新的胆管癌相关抗原(CCRA)。将人胆管癌组织匀浆经饱和硫酸铵沉淀、DE-52层析柱阶段洗脱和连续梯度洗脱、两次琼脂糖6B过滤后获得纯化的CCRA,抗原纯化程度达105.72倍,抗原活力达980.00μg/mg蛋白质;经鉴定认为CCRA是一种不同于CEA、AFP和β2-MG的一种新的肿瘤相关抗原;分子量为114×103u,蛋白电泳迁移于α2和β带之间,对胰蛋白酶和胃蛋白酶敏感,易被其破坏。免疫组化显示CCRA主要分布在胆管癌组织中,在胰腺癌和肝癌组织中为弱阳性,在其它肿瘤和正常消化道组织中无CCRA着色。A new tumor marker, cholangiocarcinoma related antigen (CCRA), a protein with a antigenic purifying degree of 105.72 fold and an antigenic activity of 980.00 μg/mg, was isolated from the tissue of human cholangiocarcinoma and purified in the following procedure: (1) The tumor tissue was firstly mixed with ammonium sulfate in 20%~45% saturation. (2) The dialyzed solution was concentrated and applied to two columns of DEAE sephacel 52 of 1.2 cm×20 cm and 1.5 cm×30 cm in size and two columns of Sepharose 6B both of 1.5 cm×70 cm in size respectively. It was identified that the purified CCRA was a new tumor related antigen which was different from carcinombryonic antigen (CEA), α fetoprotein (AFP) and β 2 microglobin (β 2 MG) and had a molecular weight of 114 kD. Electrophoresis of serum protein revealed that it was located between the α 2 and β lines. Treatment of CCRA with trypsin and pepsin resulted in loss of its immune activity, which indicates that CCRA is sensitive to and easily destroyed by the two enzymes. Immunohistochemical examination revealed that CCRA mainly existed in the tissue of cholangiocarcinoma.
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