Abstract
The availability of antisera with specificity forλ light chains which have the Mcg- or the non-Mcg-associated amino acid C-region sequence alternations has made possible our immunochemical differentiation of humanλ chains as Mcg+ or Mcg−. One antiserum, prepared against an Mcg+ λ chain having the Mcg-associated C-region amino acid residues (asparaginyl, threonyl, and lysyl at positions 116, 118, and 167, respectively), had specificity forλ chains with this C-region sequence. A second antiserum, prepared against an Mcg− λ chain having the non-Mcg-associated C-region residues (alanyl, seryl, and threonyl at these same three respective positions), had specificity forλ chains with this alternative type of C-region sequence. Immunodiffusion analyses ofλ chains of known amino acid sequence confirmed their chemical classification as Mcg or non-Mcg in type. No association between a particular V-regionλ-chain subgroup and the Mcg factor was evident. Based on sequence and serological analyses, ∼ 11 percent ofλ light chains have the Mcg-related C-region sequence alternations. The immunochemical recognition of both Mcg+ and Mcg− light chains isolated from the IgG of normal individuals corroborated the isotypic nature of the Mcg factor. Despite the fact that the Mcg-related substitutions are in the Cλ, the loss of Mcg antigenicity upon cleavage of Mcg+ and Mcg− λ chains into VL and CL indicates that the intact light polypeptide chain is essential for expression of the Mcg antigenic factor.
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Solomon, A. Bence jones proteins and light chains of immunoglobulins. Immunogenetics 5, 525–533 (1977). https://doi.org/10.1007/BF01570511
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DOI: https://doi.org/10.1007/BF01570511