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抗癌抗生素Ｃ１０２７分子由一个含１１０个氨基酸的蛋白和一个含烯二炔结构的发色团非共价结合而成。发色团是Ｃ１０２７的活性部分，易被紫外线照射灭活，蛋白则对发色团有保护作用。以紫外灭活的Ｃ１０２７为抗原，用杂交瘤技术，制备了小鼠抗Ｃ１０２７单克隆抗体Ｆ９。免疫印迹证实单抗Ｆ９能特异性识别Ｃ１０２７，该单抗对Ｃ１０２７与紫外线灭活Ｃ１０２７的亲和力无显著差别。单抗Ｆ９对Ｃ１０２７的亲和常数为２２±０４７×１０７Ｌ·ｍｏｌ－１，其亚型为ＩｇＧ１。克隆形成测定结果表明，单抗Ｆ９对Ｃ１０２７的细胞毒性无明显影响，提示该单抗没有对Ｃ１０２７的发色团产生封闭效应。ＥＬＩＳＡ与Ｗｅｓｔｅｒｎｂｌｏｔ测试说明单抗Ｆ９能与裁短的Ｃ１０２７基因工程肽发生特异性结合。提示单抗Ｆ９可用于Ｃ１０２７基因工程的研究，并可能用于研究Ｃ１０２７的代谢与分布及筛选大分子抗肿瘤抗生素等方面。
The anticancer antibiotic C1027 molecule consists of a non-covalent association of a 110 amino acid protein with a chromophore containing an enediyne structure. The chromophore is the active moiety of C1027, is easily inactivated by ultraviolet light and the protein has a protective effect on the chromophore. C1027 monoclonal antibody F9 was prepared by hybridoma technique using UV-inactivated C1027 as antigen. Immunoblotting confirmed that monoclonal antibody F9 specifically recognized C1027, and the affinity of the monoclonal antibody for C1027 and UV-inactivated C1027 was not significantly different. The affinity constant of monoclonal antibody F9 to C1027 was 2 ± 047 × 107L · mol-1 and its subtype was IgG1. The clonogenic assay showed that the monoclonal antibody F9 had no significant effect on the cytotoxicity of C1027, suggesting that the mAb did not have a blocking effect on the chromophore of C1027. ELISA and Western blot showed that mAb F9 could specifically bind to short C1027 genetically engineered peptide. It is suggested that monoclonal antibody F9 can be used in the research of C1027 gene engineering and may be used to study the metabolism and distribution of C1027 and to screen the macromolecular antitumor antibiotics.