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

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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 - Dec 1 1997

Fingerprint

Oligomerization
Immunoglobulin G
Light
Oligomers
Dialysis
Electrophoresis
Joining
Disulfides
Polyacrylamide Gel Electrophoresis
Molecules

All Science Journal Classification (ASJC) codes

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

Cite this

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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.",
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T1 - Favourable interaction between heavy and light chains arrests the undesirable oligomerization of heavy chains in the refolding of denatured and reduced immunoglobulin G

AU - Ueda, T.

AU - Maeda, Y.

AU - So, T.

AU - Imoto, T.

PY - 1997/12/1

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AB - 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.

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