Affordable Access

Oligomeric forms of single chain immunoglobulin (scIgG).

Authors
  • Schirrmann, Thomas1
  • Menzel, Christian
  • Hust, Michael
  • Prilop, Jessica
  • Jostock, Thomas
  • Dübel, Stefan
  • 1 Abteilung Biotechnologie, Institut für Biochemie und Biotechnologie, Technische Universität Braunschweig, Braunschweig, Germany. [email protected] , (Germany)
Type
Published Article
Journal
mAbs
Publisher
Landes Bioscience
Publication Date
Jan 01, 2010
Volume
2
Issue
1
Pages
73–76
Identifiers
PMID: 20081378
Source
Medline
Language
English
License
Unknown

Abstract

Assembly of immunoglobulin G (IgG) molecules from two heavy and two light chains can be facilitated by connecting the light chain to the heavy chain by an oligopeptide linker. Production of the anti-lysozyme D1.3-single chain (sc) IgG1 in HEK293T cells yielded up to 8 mg/L functional scIgG polypeptide. Size exclusion chromatography of material purified by protein-A affinity chromatography revealed that the majority of the D1.3-scIgG1 molecules were 150 kDa monomers, with a K(D) of 1.8 x 10(-10) M measured by surface plasmon resonance; however, significant fractions of scIgG dimers and oligomers with molecular masses of 300 kDa and >600 kDa, respectively, were identified. The oligomerization resulted in an increased avidity. The observed oligomerization capability may allow new approaches for the generation of bispecific/multivalent antibodies.

Report this publication

Statistics

Seen <100 times