Amino acid sequence of rabbit light chains: variable region of a light chain from a homogeneous immunoglobulin raised by streptococcal immunization

Abstract

The variable region sequence has been determined for the light chain (L) from a rabbit homogeneous immunoglobulin (3547) produced by immunization with group A streptococcal vaccine. Unlike most immunoglobulins produced by these vaccines, this immunoglobulin had no binding activity for the group A polysaccharide nor for any of a wide range of streptococcal cell components tested, nor did it have binding activity for rabbit IgG. Tryptic digestion of the citraconylated L chain and acid hydrolysis of the aspartyl-proline bond at positions 109-110 were used to obtain two variable region peptides comprising residues 1-61 and 62-109, respectively. Automated sequence analysis of these peptides and the peptides obtained from them by complete tryptic digestion gave sequence data for the entire L-chain variable (V) region. Comparison of the 3547 L chain V region sequence with other data supports the observations that only two hypervariable regions are present in rabbit kappa chains and that the hypervariable region beginning at residue 90 may vary in length by as much as six residues.

Antibody response to the streptococcal group A-variant polysaccharide in BASILEA rabbits lacking kappa-polypeptide chains.

“…The only exception was antiserum BS-4432, where the major clonotype (isoelectric point 6.1) did not bind Av-CHO. Similar observations were previously reported showing that dominant clonotypes elicited by immunization with streptococcal vaccines are not always group polysaccharide-specific antibodies (24,25). It ap- pears that a substantial number of clonotypes expressed at a low quantitative level exhibited a high antigen binding capacity, for example, the dominant clonotype of BS-4433 (pH 6.7-7.0) was compared with the discrete clonotype focusing at pH 7.5-7.9.…”

A genetic polymorphism in the constant region of rabbit b4 kappa chains.

“…A homogeneous antibody with allotype a3b4 (4539 Ab) was isolated from the transfusion plasma by DEAEcellulose chromatography and chromatography on a Group C carbohydrate immunoadsorbent column (7). Amino acid sequence studies on the light chain of 4539 Ab have been carried out using a strategy described elsewhere (8). Constant-region sequence variation was first observed upon sequence determination of a peptide (residues 110-207) isolated after acid cleavage (9) of the tryptic fragment encompassing residues 62-207.…”

Partial sequence of the variable region of an anti-p-azobenzoate antibody light chain: a one solvent sequenator program

“…Except for a threonine residue at position 50, which is also found in 2717, positions 50-52 in the Xp-1 light chain are different from all other published rabbit light-chain sequences (Jaton, 1974a,b;Chen et a]., 1975;Margolies et al, 1975;Thunberg and Kindt, 1976). Positions 50-56 are hypervariable in the light chains of other species (Wu and Kabat, 1970).…”