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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Vydáno v:	EMBO J
Hlavní autoři:	Davis, A C, Roux, K H, Pursey, J, Shulman, M J
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	Nature Publishing Group 1989
Témata:	Research Article
On-line přístup:	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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