Shalitin C
Department of Biology Technion-Israel Institute of Technology Haifa.
Yeast. 1989 Apr;5 Spec No:S525-35.
The properties of a Saccharomyces cerevisiae 20 kDa polypeptide (Yp20) and its relationship to human ras antigen were tested. Yp20 was isolated from commercial yeast cells by the procedure of Sommer (1978). Proteins associated with yeast chromatin were released by micrococcal nuclease digestion and purified by sucrose gradient centrifugation. Rabbit polyclonal and mouse monoclonal antibodies specifically detecting the Yp20 antigen have been generated. We observed that Yp20 was recognized by anti-ras polyclonal and monoclonal antibodies. Mammalian Ha-ras and Ki-ras proteins were specifically detected by anti-Yp20 antibodies. Based on immunological cross-reactivities, we believe that Yp20 may share some homology with the yeast YP2 gene previously described. Anti-Yp20 antibodies will be used to isolate the gene that encodes the protein. Practical applications of our antibodies for the detection of tumor specific antigens will be discussed.
对酿酒酵母20 kDa多肽（Yp20）的特性及其与人ras抗原的关系进行了测试。Yp20是按照Sommer（1978年）的方法从商业酵母细胞中分离出来的。与酵母染色质相关的蛋白质通过微球菌核酸酶消化释放出来，并通过蔗糖梯度离心进行纯化。已经产生了特异性检测Yp20抗原的兔多克隆抗体和小鼠单克隆抗体。我们观察到Yp20能被抗ras多克隆抗体和单克隆抗体识别。抗Yp20抗体能特异性检测哺乳动物的Ha-ras和Ki-ras蛋白。基于免疫交叉反应性，我们认为Yp20可能与先前描述的酵母YP2基因有一些同源性。抗Yp20抗体将用于分离编码该蛋白的基因。将讨论我们的抗体在检测肿瘤特异性抗原方面的实际应用。
