Light chain variable region sequence of rabbit antipneumococcal type III polysaccharide antibody 3368

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Abstract
The amino acid sequence of the amino-terminal 111 residues (variable region) for the L-chain of the homogeneous rabbit anti-pneumococcal type III polysaccharide antibody 3368 was determined. This sequence was obtained principally through automated Edman degradations of the intact L-chain and of peptides generated by tryptic digestion of the citraconylated L-chain. Only 2 .mu.mol of purified L-chain were required to determine the reported sequence. When compared with the L-chains of 4 other anti-pneumococcal type III polysaccharide antibodies, the 3368 L-chain exhibits a unique sequence in those segments of the variable region that contribute to formation of the antigen binding site (complementarity-determining regions) (10 or 11 residue differences in 12 positions). The 3368 L-chain demonstrates an insertion of 3 residues relative to the other 4 L-chains in the complementarity-determining region at positions 89-98. These 5 L-chains have greater than 80% sequence homology for the portion of the variable region which is not involved in antigen binding.
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