AN ACTIVE SINGLE-CHAIN ANTIBODY CONTAINING A CELLULASE LINKER DOMAIN IS SECRETED BY ESCHERICHIA-COLI

K TAKKINEN, ML LAUKKANEN, D SIZMANN, K ALFTHAN, T IMMONEN, L VANNE, Matti Kaartinen, JKC KNOWLES, Tuula T. Teeri

Tutkimustuotos: LehtiartikkeliArticleScientificvertaisarvioitu

Abstrakti

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 IgG1 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/l of culture medium and its affinity and stability are comparable to those of the corresponding native IgG.

AlkuperäiskieliEnglanti
Sivut837-841
Sivumäärä5
JulkaisuPROTEIN ENGINEERING
Vuosikerta4
Numero7
TilaJulkaistu - lokakuuta 1991
OKM-julkaisutyyppiA1 Julkaistu artikkeli, soviteltu

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