Diversity among Rabbit Antibody Light Chain Amino Terminal Sequences
- 1 July 1976
- journal article
- research article
- Published by The American Association of Immunologists in The Journal of Immunology
- Vol. 117 (1), 160-167
- https://doi.org/10.4049/jimmunol.117.1.160
Abstract
The amino terminal (positions 0 to 20) amino acid sequences of 22 rabbit antibody light chains are reported and compared with 44 amino terminal sequences previously described in the literature. Rabbit κ light chains demonstrate three different amino terminal chain lengths and considerable variability at the amino terminal end. In relating amino terminal sequence to b locus allotype, allotype-specific residues (amino acid residues unique to all light chains having a given allotype) were not identified, although certain residue alternatives were unique to some of the b5 and b9 light chains. There was no correlation of antibody specificity with amino terminal sequence. In the most striking example, identical amino terminal sequences were associated with two different carbohydrate specificities (type VIII pneumococcal polysaccharide and streptococcal group A carbohydrate) and an aminophenyltrimethylammonium specificity. An obligatory association of amino terminal sequence with complete variable region framework sequences was not observed. Thus, it is not always possible to predict the framework homology among a given pair of light chains by examination of their amino terminal sequences. The limited diversity seen among the variable regions of murine myelomas that have the same antigen-binding properties is not found in the light chains of specifically elicited rabbit antibodies.This publication has 2 references indexed in Scilit:
- Chemical structure of light chains: amino acid sequence of type K Bence-Jones proteinsProceedings of the Royal Society of London. B. Biological Sciences, 1966
- ANTIGEN - ANTIBODY REACTIONS IN GELS .4. TYPES OF REACTIONS IN COORDINATED SYSTEMS OF DIFFUSION1953