Chemical Analyses of Variable Regions of Heavy and Light Chains of Cold Agglutinins

J. Gergely, A. C. Wang, H. H. Fudenberg

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

Abstract. The variable regions of cold agglutinins with anti‐I and anti‐Pr specificities were investigated by N‐terminal amino acid sequencing and by analyses of pyrrolidone‐carboxylic acid‐blocked peptides after digestion of polypeptide chains with Nargase. Results showed that the heavy chains of four IgM anti‐I cold agglutinins are exclusively VHI subgroups and their light chains are exclusively VKII subgroup. In contrast, the light chains of two cold agglutinins with anti‐Pr specificity are not VKII, while their heavy chains are not restricted to a single subgroup. The amino acid sequences at the first hypervariable region of light chains (positions 25–35) are similar in two of the four anti‐I cold agglutinins. These sequences are different from that of the light chain of another cold agglutinin with anti‐Pr specificity. These results support the concept that only antibodies with the same specificity can share similar primary structure at their antigen combining sites.

Original languageEnglish
Pages (from-to)432-440
Number of pages9
JournalVox sanguinis
Volume24
Issue number5
DOIs
Publication statusPublished - May 1973

    Fingerprint

ASJC Scopus subject areas

  • Hematology

Cite this