Interaction of cupric and cadmium ions with a protein-ovalbumin (OA)
โ Scribed by S. R. Verma; J. P. S. Arora; J. S. Shankar; Dev Dutt; C. Pal
- Publisher
- Springer Netherlands
- Year
- 1989
- Tongue
- English
- Weight
- 320 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0049-6979
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โฆ Synopsis
The binding of Cu and Cd ions with ovalbumin has been measured indirectly by observing the displacement ofH รท from acidic groups on the ovalbumin. The pH-measuring procedure agreed with values obtained by an equilibrium dialysis method. Both the metals were bound by carboxyl groups with log K values being 2.39 and 2.22, respectively. The extent of binding was found to be pH dependent with the involvement of the imidazole site yielding logK values of 3.23 and 2.80, respectively. Equilibrium dialysis results supported involvement of both carboxyl and imidazole groups of the protein in metal ion binding.
๐ SIMILAR VOLUMES
## Abstract A thermodynamic study on the interaction of Jack bean urease, JBU, with Zn^2+^ and Cd^2+^ ions was studied by isothermal titration calorimetry (ITC) at 290, 300 and 310 K in 30 mmol/L Tris buffer solution, pH 7.0. The heats of JBU+Zn^2+^ and JBU+ ^2+^ interactions are reported and analy