Structural and antigenic studies of an idiotype-bearing murine antibody to the arsonate hapten.
Biochemistry, 1979/2/20;18(4):560-5.
Marchalonis JJ, Warr GW, Smith P, Begg GS, Morgan FJ
PMID: 105755
Impact factor: 3.321
Abstract
Mice of strain A/J responded to repeated intraperitoneal injection of Limulus hemocyanin derivatized with arsanilic acid by producing large quantities (approximately 5 mg/mL of ascites fluid) of IgG antibodies specific for this hapten. The antibodies possessed a characteristic idiotypic determinant and exhibited restricted heterogeneity as demonstrated by isoelectric focusing and primary N-terminal amino acid sequence analysis of isolated light and heavy polypeptide chains. Both light- and heavy-chain sequences were comparable to those of myeloma proteins in lack of heterogeneity. The N terminus of the light chain exhibited V KI sequence and only one position in the first 30 residues showed more than one amino acid. No variability was observed in the first 10 N-terminal residues of the heavy chain. Rabbit antiserum to the idiotype blocked binding of hapten by the purified antibody. The presence of both light- and heavy-chain antigenic determinants was required for optimal formation of the idiotypic determinant.
MeSH terms
Amino Acid Sequence; Amino Acids; Animals; Antibodies; Antigens, Neoplasm; Arsanilic Acid; Arsenicals; Haptens; Immunoglobulin Heavy Chains; Immunoglobulin Idiotypes; Immunoglobulin Light Chains; Immunoglobulin kappa-Chains; Mice; Mice, Inbred Strains; Radioimmunoassay
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