Thermodynamics of the binding of calcium and strontium to bovine α-lactalbumin
| Autor: | Jos A. Cox, Mladen Milos, Jean-Jacques Schaer |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
Isothermal microcalorimetry
animal structures Enthalpy Size-exclusion chromatography Biophysics chemistry.chemical_element Calorimetry Calcium Biochemistry Metal stomatognathic system Structural Biology Genetics Animals Molecular Biology Lactalbumin Strontium Ca2+ binding Chemistry virus diseases Cell Biology Sr2+ binding digestive system diseases Crystallography Microcalorimetry visual_art α-Lactalbumin Chromatography Gel visual_art.visual_art_medium Thermodynamics microcalorimetry alfa-lactalbumine Ca-binding Sr-binding Cattle Protein Binding |
| Zdroj: | FEBS Letters. 190:77-80 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(85)80431-2 |
| Popis: | Microcalorimetry and equilibrium gel filtration were used to determine the thermodynamic functions delta H degrees, delta G degrees and delta S degrees guiding the interaction of Ca2+ and Sr2+ with bovine alpha-lactalbumin. Two methods of nearly complete metal removal from the protein gave identical results. The single Ca- and Sr-binding site, which has moderate affinity for these ions (KCa = 2.5 X 10(6) M-1 and KSr = 5.1 X 10(5) M-1), displays unusually large enthalpy changes of -118 kJ X mol-1 for Ca2+ and -75 kJ X mol-1 for Sr2+. The concomitant reaction entropies equal -273 and -142 J X K-1 X mol-1, respectively. |
| Databáze: | OpenAIRE |
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