AMINO ACID SEQUENCE RESTRICTION IN RABBIT ANTIBODY LIGHT CHAINS
- 1 July 1969
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 63 (3) , 890-896
- https://doi.org/10.1073/pnas.63.3.890
Abstract
Light chains were obtained from IgG rabbit antibodies to the group-specific carbohydrates of groups A and C streptococci. An analysis of the amino acid alternatives which exist at the first three positions of the N-terminus in both light-chain preparations shows a marked restriction in amino acid sequence heterogeneity when compared with preimmune light chains. Both of these related, but immunologically distinct, antigenic determinants select the same uncommon subpopulation of rabbit light chains.Keywords
This publication has 14 references indexed in Scilit:
- RABBIT ANTIBODIES TO STREPTOCOCCAL CARBOHYDRATESThe Journal of Experimental Medicine, 1969
- Immunoglobulin Structure: Variability and HomologyScience, 1969
- THE INDIVIDUAL ANTIGENIC SPECIFICITY OF ANTIBODIES TO STREPTOCOCCAL CARBOHYDRATESThe Journal of Experimental Medicine, 1968
- Structure of Antibody MoleculesNature, 1967
- QUANTITATIVE VARIATIONS IN L CHAIN TYPES IN GUINEA PIG ANTIHAPTEN ANTIBODIESThe Journal of Experimental Medicine, 1966
- Electrophoretic Heterogeneity of Polypeptide Chains of Specific AntibodiesScience, 1966
- The amino-terminal amino acid sequences of rabbit immunoglobulin light chains.Proceedings of the National Academy of Sciences, 1966
- Hydrolysis of phenylthiohydantoins of amino acidsBiochemical and Biophysical Research Communications, 1964
- STUDIES ON THE CHEMICAL STRUCTURE OF THE STREPTOCOCCAL CELL WALLThe Journal of Experimental Medicine, 1962
- ALLOTYPY OF RABBIT SERUM PROTEINSThe Journal of Experimental Medicine, 1960