摘要单克隆抗体介导的导向显像与导向溶栓是对血栓栓塞性疾病诊断与治疗的有效手段之一。为了降低鼠源性单抗对人体的免疫原性，我们应用基因重组技术将抗人活化血小板α颗粒膜蛋白GMP-140单克隆抗体SZ-51可变区基因片段与人免疫球蛋白71重链CH1和 K轻链恒区基因进行拼接，构建噬菌体质粒（pHENl-51Fab/Hu），并导入大肠杆菌HB2151中进行表达。表达的嵌合抗体Fab片段为可溶性，经Western blot证实能特异地与GMP-140呈结合反应。经ELISA定量测定，表达上清液中的抗体含量为200μg/L。

abstractsIn order to reduce the immunogenecity of murine monoclonal antibody (mAb) to human beings, the cD-NA encoding the variable regions of mouse mAb SZ-51, which is specific against a-granule membrane pro tein (GMP) 140 on activated human platelets, was at tached to the Cκ and CHI (γ1 isotype) constant do mains of human immunoglobulin by means of recombi nant DNA technique. The phagemid construct pHENl-51Fab/Hu was obtained and introduced into non-sup pressor E. Coli strain HB2151 for expression of soluble chimeric Fab fragments. The chimeric SZ-51 Fab frag ments were proved to bind specifically to GMP-140 by western blot. The antibody concentration in the cul ture supernatant was 200μg/L measured by enzyme-linked immunosorbent assay (ELISA) .