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, whereas the heavy chains are identical throughout 45 residues of their NH2-...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1976-03, Vol.73 (3), p.923-927
Main Authors: Sledge, C., Fair, D. S., Black, B., Krueger, R. G., Hood, L.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antibodies
Antibody Formation
Antibody-Producing Cells - cytology
Antibody-Producing Cells - immunology
B lymphocytes
Cell Differentiation
Cellular immunity
Daughter cells
Genes
Humans
Immunoglobulin A - analysis
Immunoglobulin A - biosynthesis
Immunoglobulin constant regions
Immunoglobulin G - analysis
Immunoglobulin G - biosynthesis
Immunoglobulins
Lymphocytes
Models, Biological
Molecules
Myeloma Proteins - analysis
Myeloma Proteins - biosynthesis
Regional identity
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Summary: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, whereas 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 chain (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 VHregion with multiple constant regions of the heavy chain (CHregions), (ii) two alternative types of V-C joining mechanisms, (iii) the differentiation of antibody-producing cells, and (iv) three categories of biclonal immunoglobulins.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.73.3.923