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Diversity among Rabbit Antibody Light Chain Amino Terminal Sequences¹

From the Departments of Medicine and Surgery, Massachusetts General Hospital and Harvard Medical School, Boston, Mass. 02114 Chemie der Proteinen, Vrije Universiteit, Brussels, Belgium Harvard University Office of Information Technology, Cambridge, Mass. 02138

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 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.

Footnotes

¹ This work was supported by National Institutes of Health Grant A104967 and a Grant-In-Aid from the American Heart Association.

² M. N. M. is an established investigator of the American Heart Association.

³ F. W. C. is the recipient of a National Institutes of Health Training Grant 5-T01-AI-00387.