Quantitative affinity chromatography: Increased versatility of the technique for studies of ligand binding

Bergman D.A. and Winzor D.J. (1986) Quantitative affinity chromatography: Increased versatility of the technique for studies of ligand binding. Analytical Biochemistry, 153 2: 380-386. doi:10.1016/0003-2697(86)90106-5


Author Bergman D.A.
Winzor D.J.
Title Quantitative affinity chromatography: Increased versatility of the technique for studies of ligand binding
Journal name Analytical Biochemistry   Check publisher's open access policy
ISSN 1096-0309
Publication date 1986-01-01
Sub-type Article (original research)
DOI 10.1016/0003-2697(86)90106-5
Volume 153
Issue 2
Start page 380
End page 386
Total pages 7
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
Abstract The potential of affinity chromatography for the characterization of strong solute-ligand interactions is explored by studying the NADH-dependent elution of rabbit muscle lactate dehydrogenase from a column of trinitrophenyl-Sepharose in 0.067 m phosphate, pH 7.2. An interesting development is the simplification of the general affinity chromatography theory that emanates from the use of affinity matrices with a high concentration of immobilized reactant groups. The resultant expression allows evaluation of the intrinsic association constant for solute-ligand interactions from a single series of either zonal or frontal affinity chromatographic experiments conducted in the presence of a range of free ligand concentrations. Thus, contrary to previous belief, an affinity matrix designed for solute purification work should prove to be an asset for, rather than an impediment to, the study of solute-ligand interactions by quantitative affinity chromatography.
Keyword lactate dehydrogenase-NADH interaction
ligand binding
quantitative affinity chromatography
solute-ligand interactions
trypsin-p-aminobenzamidine interaction
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
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