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. 1971 Oct;68(10):2569–2573. doi: 10.1073/pnas.68.10.2569

Amino-Acid Sequences of Light Chains of a Rabbit Anti-p-Azobenzoate Antibody

E Appella *, A Chersi *, O A Roholt †, D Pressman †
PMCID: PMC389470  PMID: 5289890

Abstract

Half-cystine peptic peptides representing the intrachain disulfide bonds of the light chain from an apparently homogeneous rabbit anti-p-azobenzoate antibody were isolated in good yields after reduction and alkylation with [14C]iodoacetate, and their sequences were determined. The sequence of the first 21 amino-terminal residues was also determined. The good yields of these peptides, the fact that no variants of any of them were found, and the cleanness of the amino-terminal sequence determination confirm the high degree of homogeneity of this light-chain preparation. Previous evidence for the homogeneity of the light chain includes the appearance of only a single band upon analysis by disc electrophoresis, a relatively unique amino-acid composition, and a simple tryptic peptide map. The whole antibody shows a homogeneity of the hapten-binding constant. The antigen used in the present work is complex, since the attached hapten groups are in a large variety of environments, particularly since the carrier is a heterogeneous mixture of globulins. The very limited heterogeneity of the antibodies found in this case would appear to depend on the stimulation of only a few of the cells capable of producing antibody against a given hapten, rather than on a structural identity of the environment around each individual hapten group that is located on the antigen molecule.

Keywords: half-cystine peptic peptides, rabbit, N-terminal residues, hapten, bovine gammaglobulin

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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