Gel chromatographic evaluation of the binding constant for the interaction of thiamin diphosphate with magnesium ion

A simple gel chromatographic procedure is devised for characterizing the interactions of nucleotides and other coenzymes with metal ions. Its application is illustrated by determining the binding constant for the interaction of thiamin diphosphate with Mg 2+ ion by frontal gel chromatography on Seph...

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Bibliographic Details
Published in:Journal of Chromatography A 1992-09, Vol.609 (1), p.83-87
Main Authors: Booth, Christine K., Nixon, Peter F., Winzor, Donald J.
Format: Article
Language:English
Subjects:
Analytical chemistry
Chemistry
Exact sciences and technology
Miscellaneous
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Summary:A simple gel chromatographic procedure is devised for characterizing the interactions of nucleotides and other coenzymes with metal ions. Its application is illustrated by determining the binding constant for the interaction of thiamin diphosphate with Mg 2+ ion by frontal gel chromatography on Sephadex G-10. An association constant of 3200 (±400) M −1 is obtained for the interaction in 0.1 M Tris-HCl buffer (pH 7.6) supplemented with poly(ethylene glycol) (50 mg/ml) and mercaptoethanol (25 m M).
ISSN:0021-9673
DOI:10.1016/0021-9673(92)80151-J