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Amino acid sequence restriction in rabbit antibody light chains
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.
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.