Abstract.
Recently we developed a slow dialysis method that effectively refolds denatured and reduced immunoglobulin G (IgG) [Maeda, Ueda and Imoto (1996) Prot. Engng 9: 95-100]. 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 rejoining 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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Received 13 August 1997; received after revision 23 September 1997; accepted 1 October 1997
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Ueda, T., Maeda, Y., So, T. et al. Favourable interaction between heavy and light chains arrests the undesirable oligomerization of heavy chains in the refolding of denatured and reduced immunoglobulin G. CMLS, Cell. mol. life sci. 53, 929–934 (1997). https://doi.org/10.1007/s000180050113
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DOI: https://doi.org/10.1007/s000180050113