| Literature DB >> 11112512 |
A Schmiedl1, F Breitling, S Dübel.
Abstract
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.Entities:
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Year: 2000 PMID: 11112512 DOI: 10.1093/protein/13.10.725
Source DB: PubMed Journal: Protein Eng ISSN: 0269-2139