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Sequence Variability of Rabbit Antibody Light Chains
Author(s) -
THUNBERG A. L,
KINDT T. J.
Publication year - 1975
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1975.tb02617.x
Subject(s) - rabbit (cipher) , immunoglobulin light chain , antibody , sequence (biology) , microbiology and biotechnology , chemistry , biology , immunology , genetics , mathematics , statistics
Amino acid sequence analyses of the IgG tight (L) chains from selected members of a rabbit family with allotypes b4 and b9 showed N‐terminal substitutions that segregated with the b4 allotype. The L chains of allotype b4 had tyrosine at step 2, whereas this residue was absent from that step in the by L chains. Steps 12 and 13 of b4 L chains yielded a high percentage of glutamic acid, whereas a low percentage was observed for the b9 L chains. These tyrosine and glutamic acid substitutions were observed with the same frequency in L chains from homogeneous antibodies at in the L chains of the IgG samples. The data suggest that, in the family studied, separate and distinct V‐region gene complexes are linked to the b4 and b9 allotypic genes.