The unfolding/denaturation of immunogammaglobulin of isotype 2b and its F-ab and F-c fragments

AWP Vermeer*, W Norde, A van Amerongen

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

78 Citations (Scopus)

Abstract

The unfolding and further denaturation of IgG and its F-ab and F-c fragments were studied both on a macroscopic and molecular level, using differential scanning calorimetry and circular dichroism spectroscopy, respectively. It was shown that the structural integrity of the F-ab and F-c units was retained after fragmentation of the IgG. The F-ab fragment denatured at similar to 61 degrees C and the F-c fragment at 71 degrees C. The structural transitions observed in the whole IgG is the sum effect of those determined for the isolated F-ab and F-c fragments.

Original languageEnglish
Pages (from-to)2150-2154
Number of pages5
JournalBiophysical Journal
Volume79
Issue number4
DOIs
Publication statusPublished - Oct-2000

Keywords

  • SCANNING CALORIMETRY
  • MONOCLONAL-ANTIBODY
  • RECEPTORS
  • DOMAINS
  • IGG
  • ASSOCIATION
  • BINDING
  • SURFACE
  • FAB

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