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Cμ4 domain of IgM has cytophilic activity for human lymphocytes

Abstract

WE have isolated and identified two intact Cμ4-domain fragments from a monoclonal IgM protein. They differed only in their carbohydrate content, having the same polypeptide chain. They were separated from each other and from Fcμ monomer by molecular exclusion and affinity chromatography (insolubilised concanavalin A1) of mildly reduced and alkylated Fc5μ produced by the method of Plaut and Tomasi2. The Cμ4 fragment containing carbohydrate was designated Cμ4(+) while the carbohydrate-poor domain was called Cμ4(−). These two fragments were identified as Cμ4-domains from their amino acid sequences, amino acid compositions, molecular weights (14,700) and antigenic characteristics. Both fragments originate from tryptic cleavage at Lys-445 of the μ chain (IgM(Ou) numbering3) and could not be further fragmented by extensive reduction and alkylation4. The domain hypothesis of Edelman et al.5 proposes that each homology region of the immunoglobulins evolved to perform independent biological effector functions. Hurst et al.6 have shown that fragmented Cμ4 domain will fix activated Cl(Cl) and will also activate proenzyme Cl to Cl7. Moretta et al.8 have demonstrated receptors specific for IgM on human T lymphocytes, and this has been confirmed by McConnell and Hurd9. We now report that these receptors are specific for the Fc part of IgM (Table 1) and furthermore that the Cμ4 domain is involved in this affinity reaction in a dose-dependent manner (Fig. 1).

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CONRADIE, J., BUBB, M. Cμ4 domain of IgM has cytophilic activity for human lymphocytes. Nature 265, 160–161 (1977). https://doi.org/10.1038/265160a0

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