Binding of Cibacron Blue F3GA to Proteins Containing the Dinucleotide Fold

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1976 Feb 1

PMID 174104

Citations 34

Authors

S T Thompson

E Stellwagen

Affiliations

Soon will be listed here.

Abstract

A simple, convenient, and sensitive spectrophotometric procedure is described for quantitative measurement of nucleoside phosphate binding sites constructed by the dinucleotide fold. The procedure involves difference spectral titration of such enzymes with the dye Cibacron blue F3GA in a spectral region remote from the intrinsic absorbance of proteins or natural ligands. The titration curves can be analyzed to determine the affinity of nucleoside phosphate binding sites for both the dye and the natural ligand over a potentially wide range of experimental conditions. The interaction of the dye with two proteins which contain the dinucleotide fold, lactate dehydrogenase (L-lactate:NAD+ oxidoreductase, EC 1.1.1.27) and phosphoglycerate kinase (ATP:3-phospho-D-glycerate 1-phosphotransferase, EC 2.7.2.3), is illustrated.

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