摘要
单链抗体（ＳｃＦｖ）是一个重链可变区（ＶＨ），一个轻链可变区（ＶＬ）由连接肽（Ｌｉｎｋｅｒ）连在一起构成的单价小分子抗体。为使其能组装成双价，对一个抗人红细胞的单链抗体进行了改造，将其连接肽由１７个氨基酸〔ＳＲ（ＧＧＧＧＳ）３〕缩短为６个氨基酸（ＳＲＧＧＧＳ），强迫不同分子间的ＶＨ和ＶＬ组合成Ｆｖ，从而形成双价小分子抗体（Ｄｉａｂｏｄｙ）。在大肠杆菌中分泌型表达后，显示具有血球凝集活性，证明其为双价。进一步用凝胶过滤分析，显示改建后抗体分子的分子量约为原单链抗体的两倍。
ScFv is univalent small Ab molecule comprising a V H domain and a V L domain connected by a polypeptide linker.In order to construct bivalent molecules,we modified the anti human RBC ScFv expressing vector by shortening the linker from 17 amino acid residues SR(GGGGS) 3 to 6 amino acid residues(SRGGGS) to force the pairing of V H and V L between two different molecules to form bivalent antibody fragment(diabody).The bivalency of E.coli expressed diabody was proved by its ability to agglutinate human RBC.The dimerization of diabody was also demonstrated by gel filtration(size exclution) chromatography.
出处
《中华微生物学和免疫学杂志》
CAS
CSCD
北大核心
1997年第3期231-234,共4页
Chinese Journal of Microbiology and Immunology
