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Origin of immunoglobulin–albumin complexes

Abstract

THE propensity of human IgA and IgM monoclonal proteins to complex to endogenous serum proteins, such as albumin and α1 antitrypsin (α1AT), has been previously established1–3. When complexes of IgA-albumin and IgA-α1 antitrypsin are isolated, albumin and α1AT are found on separate polymeric IgA molecules and not on monomeric IgA3. Another polypeptide chain, J chain, has also been shown to exist in polymeric IgA and IgM (refs 4 and 5) but not monomeric immunoglobulin. Furthermore, J chain is synthesised within IgA and IgM mouse plasma cells6. Therefore, it is important to determine whether albumin is complexed to immunoglobulin as a step in intracellular biosynthesis or whether it is incorporated as a post-secretory event. We report here that IgG and IgA mouse plasmacytoma cells synthesise and secrete albumin complexed to immunoglobulin.

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HAUPTMAN, S., SOBCZAK, G. Origin of immunoglobulin–albumin complexes. Nature 263, 64–67 (1976). https://doi.org/10.1038/263064a0

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  • DOI: https://doi.org/10.1038/263064a0

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