Zhuang W Z, Kubota S, Sugimoto C, Onuma M
Department of Epizootiology, Faculty of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Parasite Immunol. 1993 Feb;15(2):113-9. doi: 10.1111/j.1365-3024.1993.tb00590.x.
Epitopes on a 32 kDa protein, which is an immunodominant major surface protein of Theileria sergenti, recognized by anti-merozoite monoclonal antibodies were characterized. The results of a competitive binding assay between monoclonal antibodies indicated that there were at least three epitopes in this protein. The presence of repeated epitopes was suggested by using two-site enzyme-linked immunosorbent assay. The protein was partitioned into the detergent phase of Triton X-114 extracts, indicating that the 32 kDa protein is an integral membrane protein. Periodate treatment of 32 kDa protein implies that one epitope of the epitopes recognized by monoclonal antibody has a carbohydrate moiety.
对一种32 kDa蛋白的表位进行了鉴定，该蛋白是瑟氏泰勒虫的一种免疫显性主要表面蛋白，可被抗裂殖子单克隆抗体识别。单克隆抗体之间的竞争性结合试验结果表明，该蛋白中至少存在三个表位。使用双位点酶联免疫吸附试验提示存在重复表位。该蛋白被分配到Triton X-114提取物的去污剂相中，表明32 kDa蛋白是一种整合膜蛋白。对32 kDa蛋白进行高碘酸盐处理表明，单克隆抗体识别的表位中有一个具有碳水化合物部分。
