ISSN:
1420-9071
Keywords:
Key words. Aggregation; H chain; immunoglobulin G; L chain; protein folding; slow dialysis.
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s000180050113
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