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

研究成果: ジャーナルへの寄稿学術誌査読

3 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)929-934
ページ数6
ジャーナルCellular and Molecular Life Sciences
53
11-12
DOI
出版ステータス出版済み - 1997

!!!All Science Journal Classification (ASJC) codes

  • 分子医療
  • 分子生物学
  • 薬理学
  • 細胞および分子神経科学
  • 細胞生物学

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