An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coli

Kristiina Takkinen, Marja-Leena Laukkanen, Dorothea Sizmann, Kaija Alfthan, Tiina Immonen, Liisa Vanne, Matti Kaartinen, Jonathan Knowles, Tuula Teeri (Corresponding Author)

    Research output: Contribution to journalArticleScientificpeer-review

    94 Citations (Scopus)

    Abstract

    Single-chain antibodies consist of the variable, antigen-binding domains of antibodies joined to a continuous polypeptide by genetically engineered peptide linkers. We have used the flexible interdomain linker region of a fungal cellulase to link together the variable domains of an anti-2-phenyloxazolone IgGl and show here that the resulting single-chain antibody is efficiently secreted and released to the culture medium of Escherichia coli. The yield of affinity-purified single-chain antibody is 1 -2 mg/1 of culture medium and its affinity and stability are comparable to those of the corresponding native IgG.

    Original languageEnglish
    Pages (from-to)837 - 841
    Number of pages5
    JournalProtein Engineering
    Volume4
    Issue number7
    DOIs
    Publication statusPublished - 1991
    MoE publication typeA1 Journal article-refereed

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