Spectroscopic and kinetic studies of the active site of anti-trinitrophenyl antibodies

Ronald P. Taylor, Richard L Riley, Daniel J. Weber

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

The titer of high affinity anti-trinitrophenyl antibodies can be determined by two different spectroscopic methods. A fluorescence approach, based on the approx 10-fold increase in fluorescence of the probe, 1,1-dihydro, 2,4,6-trinitrocyclohexadienate, on binding to homologous antibody has been used to titrate both specifically purified antibodies and an IgG subfraction. We have simplified a previously published method, based on the observation that these antibodies cause the breakdown of complexes formed between trinitrophenyl amino acids and sulfite. A study of the kinetic aspects of this latter reaction indicates the rate-determining step in the reaction is the dissociation of the hapten-sulfite complex. This suggests the antibody can bind to free hapten, but not to the hapten-sulfite complex.

Original languageEnglish
Pages (from-to)227-229
Number of pages3
JournalImmunochemistry
Volume14
Issue number3
DOIs
StatePublished - Jan 1 1977
Externally publishedYes

Fingerprint

Sulfites
Haptens
Anti-Idiotypic Antibodies
Catalytic Domain
Antibodies
Fluorescence
Immunoglobulin G
Amino Acids

ASJC Scopus subject areas

  • Molecular Biology
  • Immunology

Cite this

Spectroscopic and kinetic studies of the active site of anti-trinitrophenyl antibodies. / Taylor, Ronald P.; Riley, Richard L; Weber, Daniel J.

In: Immunochemistry, Vol. 14, No. 3, 01.01.1977, p. 227-229.

Research output: Contribution to journalArticle

Taylor, Ronald P. ; Riley, Richard L ; Weber, Daniel J. / Spectroscopic and kinetic studies of the active site of anti-trinitrophenyl antibodies. In: Immunochemistry. 1977 ; Vol. 14, No. 3. pp. 227-229.
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