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Antibody differentiation: Apparent sequence identity between variable regions shared by IgA and IgG immunoglobulins

Sledge, C. and Fair, D. S. and Black, B. and Krueger, R. G. and Hood, L. (1976) Antibody differentiation: Apparent sequence identity between variable regions shared by IgA and IgG immunoglobulins. Proceedings of the National Academy of Sciences of the United States of America, 73 (3). pp. 923-927. ISSN 0027-8424. doi:10.1073/pnas.73.3.923.

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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 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.

Item Type:Article
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Hood, L.0000-0001-7158-3678
Additional Information:© 1976 by the National Academy of Sciences. Communicated by William B. Wood, December 15, 1975. This work was supported by grants from the National Science Foundation and the National Institutes of Health. L.H. has a Research Career Development Award from NIH.
Subject Keywords:automatic sequenator; differentiation; variable-constant joining mechanisms; categories of biclonal immunoglobulins
Issue or Number:3
Record Number:CaltechAUTHORS:SLEpnas76
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:7711
Deposited By: Tony Diaz
Deposited On:01 Aug 2007
Last Modified:08 Nov 2021 20:45

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