Evidence for Control of Synthesis of the Variable Regions of the Heavy Chains of Immunoglobulins G and M by the Same Gene
Author(s) -
A. C. Wang,
S. K. Wilson,
John E. Hopper,
H. Hugh Fudenberg,
Alfred Nisonoff
Publication year - 1970
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.66.2.337
Subject(s) - immunoglobulin light chain , antibody , clone (java method) , immunoglobulin heavy chain , gene , amino acid , biology , genetics , chemistry , microbiology and biotechnology
Previous work indicated that the light chains of a monotypic immunoglobulins G2-K and M-K from a single patient (Ti1) are identical. Our present data show that the monotypic immunoglobulins G and M share idiotypic determinants not present in their isolated light chains or in any of a large number of other immunoglobulins tested, and that amino acid sequences of the first 27 residues from the NH(2)-terminal end of the gamma- and mu-chains are identical. These results support the hypothesis that at least two genes control the synthesis of each heavy and light chain and suggest that the monotypic immunoglobulin G and monotypic immunoglobulin M of this patient share three of the four genes involved. It is proposed that, during normal immunoglobulin synthesis, different cells of a single clone synthesize immunoglobulins M and G, and that the light chains and the variable segments of the heavy chains of the proteins of the two classes are identical within the clone. A genetic switching mechanism is suggested.
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