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Carl B

Carl Borrebaeck

Professor

Carl B

Kinetic analysis of recombinant antibody-antigen interactions : Relation between structural domains and antigen binding

Author

  • Carl A K Borrebaeck
  • Ann-Christin Malmborg Hager
  • Christina Furebring
  • Anne Michaelsson
  • Sally Ward
  • Lena Danielsson
  • Mats Ohlin

Summary, in English

The relation between domain structures of recombinant monoclonal antibody fragments and their reaction kinetics was studied for the first time using a novel biosensor based on surface plasmon resonance technology. The association and dissociation rate constants of Fab, Fv and single domain (VH fragment) anti-lysozyme antibodies were determined and compared to the intact monoclonal antibody. Fab and Fv fragments showed similar reaction kinetics and had affinity constants of 6 X 109 M-1 and 25 X 109 M-1, respectively. The single domain antibody had significantly different reaction kinetics compared to the fragments consisting of paired heavy and light chain domains. The VH domain had both a higher dissociation and a lower association rate constant, which resulted in an affinity constant approximately 250 times lower than the Fab fragment. This rapid evaluation of antibody reaction kinetics should prove to be an important selection parameter when comparing antibody fragments for their utility in therapeutic or other applications.

Department/s

  • Department of Immunotechnology

Publishing year

1992

Language

English

Pages

697-698

Publication/Series

Bio/Technology

Volume

10

Issue

6

Document type

Journal article

Publisher

Nature Publishing Group

Status

Published

ISBN/ISSN/Other

  • ISSN: 0733-222X