Light Chain Sequences of Human IgM Cold Agglutinins

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 69; no. 1; pp. 40 - 43
• Main Authors: Capra, J. Donald, Kehoe, J. Michael, Williams, Ralph C., Feizi, Ten, Kunkel, Henry G.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 01.01.1972; National Acad Sciences
• Subjects: Agglutinins; Amino Acid Sequence; Amino acids; Antibodies; Antibodies - analysis; Antibodies - isolation & purification; Antigens; Biochemistry; Biological Sciences: Immunology; Blood Protein Electrophoresis; Chromatography, Gel; Electrophoresis; Epitopes; Humans; Immunochemistry; Immunodiffusion; Immunoglobulins; Immunoglobulins - analysis; Immunoglobulins - isolation & purification; Peptides - analysis; Protein Conformation; Proteins
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.69.1.40

The amino-terminal amino-acid sequence has been determined for the kappa light chains of nine IgM cold agglutinins with specificity for blood group-related carbohydrate antigens. Six of the nine sequences corresponded to the prototype VKIIIsubgroup pattern, two to that of subgroup VKII, and only one to the VKIsubgroup. This distribution of kappa subgroups differs markedly from that of normal and myeloma proteins sequenced to date, where the VKIsubgroup is more prevalent than either VKIIor VKIII. Evidence is presented that supports the conclusion that the unusual subgroup distribution relates to the antibody property itself and not to some other attribute of these molecules.