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

作者信息

Takkinen K, Laukkanen M L, Sizmann D, Alfthan K, Immonen T, Vanne L, Kaartinen M, Knowles J K, Teeri T T

机构信息

VTT Biotechnical Laboratory, Espoo, Finland.

出版信息

Protein Eng. 1991 Oct;4(7):837-41. doi: 10.1093/protein/4.7.837.

DOI:10.1093/protein/4.7.837
PMID:1798707
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 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.

摘要

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