Is Ca(II) ion binding to prothrombin fragment 1 intrinsically cooperative, or is the cooperative binding accounted for by self-association?
| Autor: | Dougald M. Monroe, R. G. Hiskey, David W. Deerfield, S. Cabaniss, L. G. Pedersen |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
genetic structures
Cations Divalent Macromolecular Substances Allosteric regulation chemistry.chemical_element Cooperativity Protein aggregation Calcium Ion Ion binding Animals Protein Precursors Equilibrium constant Chemistry Cooperative binding Hematology General Medicine Peptide Fragments Models Chemical Biochemistry Biophysics Thermodynamics Cattle Prothrombin Dialysis Mathematics Protein Binding |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 0957-5235 |
| DOI: | 10.1097/00001721-199507000-00015 |
| Popis: | The recent suggestion that the apparent cooperativity seen in the binding of Ca(II) ions to prothrombin fragment 1 is due to protein aggregation is evaluated. Since (1) we find that the Ca(II) ion binding is not dependent upon protein concentration, (2) the analytical expression for the equilibrium constant of the aggregation model is unrealistically large when evaluated at realistic Ca(II) ion concentrations, and (3) a very simple allosteric cooperative binding model (Monod) can be shown to fit the experimental data, we conclude that the aggregation explanation for the apparent cooperativity in the Ca(II) ion binding by prothrombin fragment 1 is not correct. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|