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Interdomain disulfide bond of a homogeneous rabbit pneumococcal antibody light chain

Academic Article
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Overview

authors

  • Strosberg, Donny
  • Margolies, M. N.
  • Haber, E.

publication date

  • 1975

journal

  • Journal of Immunology  Journal

abstract

  • Rabbit light chain 3315, prepared from a homogeneous antipneumococcal antibody, was subjected to hydrolysis by pepsin without prior reduction and alkylation of the intrachain disulfide bonds. Gel filtration of the hydrolysate on Sephadex G-10, G-15, and G-25 and ion exchange chromatography on SP-Sephadex yielded several disulfide bridge peptides. These were fully reduced and alkulated and sequenced by Edman degradation. The peptides were located in the light chain sequence determined in independent studies from our laboratory. The half-cystine residues in this KB rabbit chain are located at positions 23, 80, 88, 134, 171, 194, and 214. The extra disulfide bridge extends between residues 80 and 171, thus joining the variable and constant domains. This is consistent with x-ray diffraction crystallographic studies showing that the corresponding residues in human light chains are separated by a distance compatible with disulfide bond formation.

subject areas

  • Amino Acid Sequence
  • Animals
  • Antibodies, Bacterial
  • Disulfides
  • Immunoglobulin Light Chains
  • Nitroprusside
  • Pepsin A
  • Peptides
  • Rabbits
  • Streptococcus pneumoniae
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Identity

International Standard Serial Number (ISSN)

  • 0022-1767

PubMed ID

  • 240892
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Additional Document Info

start page

  • 1422

end page

  • 1424

volume

  • 115

issue

  • 5

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