Table 2. Association constants and thermodynamic data for binding of creatinine to HSA.
Condition | Ka[M−1] | n | ΔGa[Kcal/mol] | ΔHa[Kcal/mol] | ΔSa[cal/mol/K] | ||
ITCa | Specb | ITCa | Specb | ||||
A | 8.92×104 | *1.15×104 #2.92×104 | 0.98 | *0.94#1.07 | −6.75 | −0.017±0.91 | 22.6 |
B | 2.69×105 | *9.76×105 #1.36×105 | 0.94 | *1.29#1.17 | −23.03 | −15.53±0.79 | −25.2 |
Condition A: N Isomer of HSA at pH 7.0+ CTN.
Condition B: B Isomer of HSA at pH 9.0+ CTN.
Constants determined by Isothermal Titration Calorimetry.
Constants determined by Fluorescence spectroscopy (*λexcitation = 280 nm; #λexcitation = 295 nm).