Amino acid sequence of the variable domains of a human anti-Rh(c) antibody: presence of an unusually long CDR3 in the lambda chain. Academic Article uri icon

Overview

abstract

  • The complete amino acid sequence of the lambda light chain and the variable domain of the heavy chain of an anti-Rh(c) human monoclonal antibody were determined. The lambda chain presents a long third complementarity-determining region sequence with unusual amino acid insertions at the C-terminus. The proposed sequence indicates that this lambda chain may be assigned to the variable region subgroup I. The J segment is identical to that of J lambda 2 except for the first amino acid residue. Positions 152 (serine) and 190 (arginine) from this sequence correspond to the Kern-Oz- isotype, respectively. The VH segment can be classified as a VHIII subgroup member. The CDR1 segment of the anti-Rh(c) VH region has the same sequence as the VH of human BRO protein except for the first residue of the CDR1. The amino acid sequence of the anti-Rh(c) D segment does not match any published D segment. The JH segment used in this protein can be classified as a JH3 with a single amino acid difference at the fourth residue.

publication date

  • December 1, 1989

Research

keywords

  • Immunoglobulin Variable Region
  • Immunoglobulin lambda-Chains
  • Isoantibodies

Identity

Scopus Document Identifier

  • 0024847733

Digital Object Identifier (DOI)

  • 10.1016/0161-5890(89)90062-x

PubMed ID

  • 2517316

Additional Document Info

volume

  • 26

issue

  • 12