An equilibrium dialysis technique for examining magnesium binding to macromolecules is described. The technique is used to determine the binding constants of magnesium to human prothrombin. This procedure should be of great utility for many biochemical systems which exhibit magnesium affinity.
Determination of strontium binding to macromolecules
โ Scribed by Nam-Won Huh; Pola Berkowitz; Richard G. Hiskey; Lee G. Pedersen
- Book ID
- 102630684
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- English
- Weight
- 353 KB
- Volume
- 198
- Category
- Article
- ISSN
- 0003-2697
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โฆ Synopsis
An equilibrium dialysis technique for determining the binding of strontium to macromolecules is described. The major difficulty to be overcome is that 90Sr has a decay product, 90Y, which is also a beta-emitter. The described protocol is used to determine the Sr binding isotherm to bovine prothrombin fragment 1. The binding is found to be cooperative, somewhat weaker than Ca binding, and to involve approximately nine strontium sites. The stoichiometric equilibrium constants are determined by nonlinear regression. The procedure should be of great utility for many macromolecules that show strontium affinity.
๐ SIMILAR VOLUMES
A new method has been developed for determining macroscopic binding constants of a few surfactants to some macromolecules. Then, the binding of ionic surfactants (cetyltrimethyl ammonium bromide, tetradecyltrimethyl ammonium bromide, and sodium tetradecyl sulfate) [STS]) to macromolecules (bovine se