Favourable interaction between heavy and light chains arrests the undesirable oligomerization of heavy chains in the refolding of denatured and reduced immunoglobulin G

T. Ueda, Y. Maeda, T. So, T. Imoto

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Recently we developed a slow dialysis method that effectively refolds denatured and reduced immunoglobulin G (IgG). This method allows both individual and simultaneous refolding of denatured and reduced H and L chains. Analysis by SDS-polyacrylamide gel electrophoresis revealed that some oligomers were formed through disulfide bonds when H chains were refolded individually. It was also shown that the extent of IgG obtained by joining the mixture of refolded H and L chains which had been refolded individually was similar to that obtained by refolding denatured and reduced whole IgG. The results indicated that a favourable interaction between H and L chains prevented formation of H-chain oligomers to yield intact IgG. The present results suggest a mechanism whereby individually folded chains might associate to form IgG molecules in vivo.

Original languageEnglish
Pages (from-to)929-934
Number of pages6
JournalCellular and Molecular Life Sciences
Volume53
Issue number11-12
Publication statusPublished - 1997 Dec 1

Keywords

  • Aggregation
  • H chain
  • Immunoglobulin G
  • L chain
  • Protein folding
  • Slow dialysis

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Cellular and Molecular Neuroscience
  • Cell Biology

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