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Structure and specificity of guinea pig 7S antibodies

Academic Article
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Overview

authors

  • Edelman, Gerald
  • Ovary, Z.
  • Benacerraf, B.

publication date

  • 1963

journal

  • Journal of Experimental Medicine  Journal

abstract

  • Additional evidence has been obtained to show that different guinea pig anti-hapten antibodies differ in the structure of their L polypeptide chains. Antibodies from animals immunized with the same hapten conjugated to different carrier proteins gave similar starch gel electrophoretic patterns after dissociation of their chains. In a study of fine differences of specificity, cross-reacting antibodies were found to have some L chains with the same electrophoretic mobility. The multiplicity of L chain bands found in the characteristic starch gel electrophoretic patterns of dissociated anti-DNP antibodies was shown to be a reflection of the heterogeneity of antibodies of slightly different specificities. Reduction and alkylation of the active fragment produced by digestion of antibodies with papain yielded starch gel electrophoretic bands corresponding in mobility to L chains. The results are consistent with the notion that L chains are involved in the acquisition of immunologic specificity.

subject areas

  • Animals
  • Antibodies
  • Guinea Pigs
  • Haptens
  • Immunization
  • Immunodiffusion
  • Immunoelectrophoresis
  • Peptides
  • Research
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Identity

PubMed Central ID

  • PMC2137705

International Standard Serial Number (ISSN)

  • 0022-1007

Digital Object Identifier (DOI)

  • 10.1084/jem.118.2.229

PubMed ID

  • 14074387
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Additional Document Info

start page

  • 229

end page

  • 244

volume

  • 118

issue

  • 2

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