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

被引：103

作者：

TAKKINEN, K ^{[1
]}

LAUKKANEN, ML ^{[1
]}

SIZMANN, D ^{[1
]}

ALFTHAN, K ^{[1
]}

IMMONEN, T ^{[1
]}

VANNE, L ^{[1
]}

KAARTINEN, M ^{[1
]}

KNOWLES, JKC ^{[1
]}

TEERI, TT ^{[1
]}

机构：

[1] TECH RES CTR FINLAND, BIOTECH LAB, POB 202, SF-02151 ESPOO, FINLAND

来源：

PROTEIN ENGINEERING | 1991年 / 4卷 / 07期

关键词：

CELLULASE LINKER PEPTIDE; ESCHERICHIA-COLI; EXTRACELLULAR PRODUCTION; SINGLE-CHAIN ANTIBODY; VARIABLE DOMAINS;

D O I：

10.1093/protein/4.7.837

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：837 / 841

页数：5

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