免疫原性
重组DNA
亲和层析
大肠杆菌
周质间隙
抗体
分子生物学
化学
抗原
生物化学
生物
酶
基因
遗传学
免疫学
作者
Andreas Schmiedl,Frank Breitling,Stefan Dübel
出处
期刊:Protein Engineering Design & Selection
[Oxford University Press]
日期:2000-10-01
卷期号:13 (10): 725-734
被引量:42
标识
DOI:10.1093/protein/13.10.725
摘要
A bispecific disulfide-stabilized Fv antibody fragment (dsFv-dsFv') consisting of two different disulfide-stabilized Fv antibody fragments connected by flexible linker peptides was produced by secretion of three polypeptide chains into the periplasm of Escherichia coli. The dsFv-dsFv' molecules were enriched by immobilized metal affinity chromatography and further purified by anion-exchange chromatography. The recombinant antibody constructs retained the two parental antigen binding specificities and were able to cross-link the two different antigens. The described dsFv-dsFv' design might be of particular value for therapeutic in vivo applications since improved stability is expected to be combined with minimal immunogenicity.
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