An Active Single-chain Antibody Containing a Cellulase Linker Domain is Secreted by Escherichia Coli

Overview

Journal Protein Eng

Publisher Oxford University Press

Specialties Biochemistry
Biotechnology

Date 1991 Oct 1

PMID 1798707

Citations 22

Authors

K Takkinen

M L Laukkanen

D Sizmann

K Alfthan

T Immonen

L Vanne

M Kaartinen

J K Knowles

T T Teeri

Affiliations

Soon will be listed here.

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.

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