期刊论文详细信息
FEBS Letters | |
Thermodynamics of the binding of calcium and strontium to bovine α‐lactalbumin | |
Milos, Mladen1  Cox, Jos A.2  Schaer, Jean-Jacques1  | |
[1] Department of Physical Chemistry, University of Geneva, 30, quai Ernest-Ansermet. 1211 Geneva 4, Switzerland;Department of Biochemistry, University of Geneva, 30, quai Ernest-Ansermet. 1211 Geneva 4, Switzerland | |
关键词: Microcalorimetry; α-Lactalbumin; Ca2+ binding; Sr2+ binding; | |
DOI : 10.1016/0014-5793(85)80431-2 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Microcalorimetry and equilibrium gel filtration were used to determine the thermodynamic functions ΔH°, ΔG° and ΔS° guiding the interaction of Ca2+ and Sr2+ with bovine α-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 (K ca = 2.5 × 106 M−1 and K Sr = 5.1 × 105 M−1), displays unusually large enthalpy changes of −118 kJ · mol−1 for Ca2+ and −75 kJ·mol−1 for Sr2+. The concomitant reaction entropies equal −273 and −142 J·K−1· mol−1, respectively.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912020287186ZK.pdf | 409KB | download |