Measurement of binding constants for divalent antibody-immobilized antigen interaction by antigen-sepharose 4b chromatography

María Rut Bruera, Daniel Sevlever, Carlos A. Gatti

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Binding constants for the human IgG-anti human IgG heavy chain were determined from elution profiles obtained by loading human IgG-Sepharose 4B columns with the antibody and eluting it at different NaI concentrations. The agreement between the value obtained at zero NaI concentration and the value determined in solution by equilibrium molecular sieving was good. An application of this column method should be useful for comparison of avidity values of antibody populations of the same specificity.

Original languageEnglish (US)
Pages (from-to)529-538
Number of pages10
JournalImmunological Investigations
Volume12
Issue number5
DOIs
StatePublished - 1983
Externally publishedYes

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Immobilized Antibodies
Agarose Chromatography
Sepharose
Antigens
Antibody Affinity
Immunoglobulin G
Antibodies
Population

ASJC Scopus subject areas

  • Immunology

Cite this

Measurement of binding constants for divalent antibody-immobilized antigen interaction by antigen-sepharose 4b chromatography. / Bruera, María Rut; Sevlever, Daniel; Gatti, Carlos A.

In: Immunological Investigations, Vol. 12, No. 5, 1983, p. 529-538.

Research output: Contribution to journalArticle

Bruera, María Rut ; Sevlever, Daniel ; Gatti, Carlos A. / Measurement of binding constants for divalent antibody-immobilized antigen interaction by antigen-sepharose 4b chromatography. In: Immunological Investigations. 1983 ; Vol. 12, No. 5. pp. 529-538.
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