Cyanide ion was studied as an effector of Jack bean urease(JBU) at 300 K in 30 mmol/LTris buffer,pH 7 by isothermal titration calorimetry(ITC).The simple novel model was used for CN^- + JBU interaction over the whole ...Cyanide ion was studied as an effector of Jack bean urease(JBU) at 300 K in 30 mmol/LTris buffer,pH 7 by isothermal titration calorimetry(ITC).The simple novel model was used for CN^- + JBU interaction over the whole range of CN^- concentrations.The binding parameters recovered from the simple novel model were attributed to the cyanide ion interaction.It was found that cyanide ion acted as a noncooperative inhibitor of JBU,and there is a set of 12 identical and independent binding sites for CN^- ions.The di...展开更多
Cyanide ion was studied as an inhibitor of Jack bean urease at 300 K in 30 mmol/L tris buffer, pH 7. The inhibition was investigated by isothermal titration calorimetry （ITC）. The extended solvation model was used f...Cyanide ion was studied as an inhibitor of Jack bean urease at 300 K in 30 mmol/L tris buffer, pH 7. The inhibition was investigated by isothermal titration calorimetry （ITC）. The extended solvation model was used for CN^- ＋ JBU interaction over the whole range of CN^- concentrations. The binding parameters recovered from the solvation model were attributed to the cyanide ion interaction. It was found that cyanide ion acted as a non-cooperative inhibitor ofurease, and there is a set of 12 ± 0.12 identical and independent binding sites for CN- ions. The dissociation equilibrium constant is 749.99 umol/L. The molar enthalpy of binding is AH= -13.60 kJ mol^-1.展开更多
The interaction of human serum albumin with divalent nickel ion was studied by equilibrium dialysis, isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC) and circular dichroism (CD) in 30 mm...The interaction of human serum albumin with divalent nickel ion was studied by equilibrium dialysis, isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC) and circular dichroism (CD) in 30 mmol/L Tris buffer , pH=7 0. There is a set of 8 identical binding sites for nickel binding on the protein at two temperatures of 300 K and 310 K. The cooperativity in the binding is observed at 310 K. The Hill coefficients at 300 K and 310 K are 0 97 and 1 25, respectively. The interaction between nickel ions and HSA is exothermic. A value of -36 5 kJ for enthalpy of interaction ( 1∶1 stoichiometry) was obtained. The secondary structure of HSA dose not show any change during the binding nickel ions process. However, the tertiary structure of the protein changes, which shows the existence of two natives like states.展开更多
A thermodynamic study on the interaction of myelin basic protein with mercury ion was studied by using isothermal titration calonmetry,ITC,at 300.15,310.15 and 320.15 K in Tris buffer solution at pH 7.The enthalpies o...A thermodynamic study on the interaction of myelin basic protein with mercury ion was studied by using isothermal titration calonmetry,ITC,at 300.15,310.15 and 320.15 K in Tris buffer solution at pH 7.The enthalpies of MBP ＋ Hg^（2＋） interaction are reported and analysed in terms of the extended solvation model.It was found that MBP has two identical and non-cooperative binding sites for Hg^（2＋） ions.The intrinsic dissociation equilibrium constants are 99.904,112.968 and 126.724μmol/L,and the molar enthalpy of binding are -11.634,-10.768 and -10.117kJ mol^（-1） at 300.15,310.15 and 320.15 K,respectively.展开更多
文摘Cyanide ion was studied as an effector of Jack bean urease(JBU) at 300 K in 30 mmol/LTris buffer,pH 7 by isothermal titration calorimetry(ITC).The simple novel model was used for CN^- + JBU interaction over the whole range of CN^- concentrations.The binding parameters recovered from the simple novel model were attributed to the cyanide ion interaction.It was found that cyanide ion acted as a noncooperative inhibitor of JBU,and there is a set of 12 identical and independent binding sites for CN^- ions.The di...
文摘Cyanide ion was studied as an inhibitor of Jack bean urease at 300 K in 30 mmol/L tris buffer, pH 7. The inhibition was investigated by isothermal titration calorimetry （ITC）. The extended solvation model was used for CN^- ＋ JBU interaction over the whole range of CN^- concentrations. The binding parameters recovered from the solvation model were attributed to the cyanide ion interaction. It was found that cyanide ion acted as a non-cooperative inhibitor ofurease, and there is a set of 12 ± 0.12 identical and independent binding sites for CN- ions. The dissociation equilibrium constant is 749.99 umol/L. The molar enthalpy of binding is AH= -13.60 kJ mol^-1.
文摘The interaction of human serum albumin with divalent nickel ion was studied by equilibrium dialysis, isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC) and circular dichroism (CD) in 30 mmol/L Tris buffer , pH=7 0. There is a set of 8 identical binding sites for nickel binding on the protein at two temperatures of 300 K and 310 K. The cooperativity in the binding is observed at 310 K. The Hill coefficients at 300 K and 310 K are 0 97 and 1 25, respectively. The interaction between nickel ions and HSA is exothermic. A value of -36 5 kJ for enthalpy of interaction ( 1∶1 stoichiometry) was obtained. The secondary structure of HSA dose not show any change during the binding nickel ions process. However, the tertiary structure of the protein changes, which shows the existence of two natives like states.
文摘A thermodynamic study on the interaction of myelin basic protein with mercury ion was studied by using isothermal titration calonmetry,ITC,at 300.15,310.15 and 320.15 K in Tris buffer solution at pH 7.The enthalpies of MBP ＋ Hg^（2＋） interaction are reported and analysed in terms of the extended solvation model.It was found that MBP has two identical and non-cooperative binding sites for Hg^（2＋） ions.The intrinsic dissociation equilibrium constants are 99.904,112.968 and 126.724μmol/L,and the molar enthalpy of binding are -11.634,-10.768 and -10.117kJ mol^（-1） at 300.15,310.15 and 320.15 K,respectively.
