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

Research output: Contribution to journalArticleScientificpeer-review

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.

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

Keywords

  • CELLULASE LINKER PEPTIDE
  • ESCHERICHIA-COLI
  • EXTRACELLULAR PRODUCTION
  • SINGLE-CHAIN ANTIBODY
  • VARIABLE DOMAINS
  • X-RAY-SCATTERING
  • TRICHODERMA-REESEI
  • CELLOBIOHYDROLASE-II
  • PROTEINS
  • GENE
  • EXPRESSION
  • SEQUENCE
  • VECTORS
  • FRAGMENT
  • PRODUCT

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