Intermolecular disulfide bonding in IgM: effects of replacing cysteine residues in the mu heavy chain.

The conventional model of polymeric IgM depicts a unique structure in which the mu heavy chains and J chain are joined by well defined disulfide bonds involving cysteine residues at positions 337, 414 and 575 of the mu chain. To test this model, we have used site directed mutagenesis to produce IgM...

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Detalles Bibliográficos
Publicado en:EMBO J
Autores principales: Davis, A C, Roux, K H, Pursey, J, Shulman, M J
Formato: Artigo
Lenguaje:Inglês
Publicado: Nature Publishing Group 1989
Materias:
Research Article
Acceso en línea:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC401247/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2511005/
https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1989.tb08389.x
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