Natori T, Law L W, Appella E
Cancer Res. 1978 Feb;38(2):359-64.
We reported previously the partial purification of detergent-solubilized specific tumor rejection antigen of a chemically induced sarcoma, Meth-A. During the course of the study, rabbit antiserum against a partially purified specific tumor rejection antigen preparation was raised and rendered specific by in vivo absorption. In this report we show that an antigenic molecule defined by in vivo-absorbed rabbit antiserum, which we tentatively refer to as tumor-specific surface antigen, was solublized by detergent Nonidet P40, and extensive attempts at purification were carried out by a sequence of procedures including gel filtration, isotachophoresis, and polyacrylamide gel electrophoresis. The most highly purified tumor-specific surface antigen retained some specific tumor rejection antigen activity, suggesting an association of the two activities. Both antigens were shown to have a molecular weight of about 60,000 and an electrophoretic mobility of alpha-globulin.
我们先前报道了对化学诱导的肉瘤Meth-A的去污剂溶解的特异性肿瘤排斥抗原进行部分纯化的情况。在研究过程中,制备了针对部分纯化的特异性肿瘤排斥抗原制剂的兔抗血清,并通过体内吸收使其具有特异性。在本报告中,我们表明,一种由体内吸收的兔抗血清所定义的抗原分子(我们暂将其称为肿瘤特异性表面抗原)可被去污剂Nonidet P40溶解,并通过包括凝胶过滤、等速电泳和聚丙烯酰胺凝胶电泳在内的一系列程序进行了广泛的纯化尝试。纯化程度最高的肿瘤特异性表面抗原保留了一些特异性肿瘤排斥抗原活性,这表明两种活性之间存在关联。两种抗原的分子量均约为60,000,电泳迁移率为α球蛋白。