Antibody differentiation: apparent sequence identity between variable regions shared by IgA and IgG immunoglobulins.
We have analyzed a pair of human myeloma immunoglobulins (biclonal proteins) of the IgG and IgA classes from a single patient, GR. The light chains are identical in amino-acid sequence over 40 residues at their NH2-terminus, hwereas the heavy chains are identical throughout 45 residues of their NH2-terminus. Additional chemical and serological studies suggest the light chains and variable regions of the heavy chains (VH) are very similar, if not identical. The implications of these and of other published studies are discussed with regard to (i) the association of one VH region with multiple constant regions of the heavy chain (CH regions), (ii) two alternative types of V-C joining mechanisms, (iii) the differentiation of antibody-producing cells, and (iv) three categories of biclonal immunoglobulins.
D000595:Amino Acid Sequence; D000917:Antibody Formation; D000921:Antibody-Producing Cells / Q000166:cytology / Q000276:immunology; D002454:Cell Differentiation; D005796:Genes; D006801:Humans; D007070:Immunoglobulin A / Q000032:analysis / Q000096:biosynthesis*; D007074:Immunoglobulin G / Q000032:analysis / Q000096:biosynthesis*; D008954:Models, Biological; D009194:Myeloma Proteins / Q000032:analysis / Q000096:biosynthesis*
D007070:Immunoglobulin A; D007074:Immunoglobulin G; D009194:Myeloma Proteins