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Abstract
Intact Cμ4-domain was isolated by molecular exclusion chromatography of reduced and alkylated Fo5μ prepared by tryptic digestion at 60°C of a monoclonal IgM. Two fragments were obtained of which one contained carbohydrate and the other none. These fragments were successfully separated by chromatography on insolubilised Concanavalin A. Cμ4-domain was identified by means of amino acid sequence, amino acid composition, molecular weight and immunological analyses. It has a molecular weight of 14,700 daltons and results from tryptic cleavage at Lys-445 of the μ-chain.