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- W2040389986 abstract "Thermodynamic parameters were determined for the thermal denaturation of Ca2+-bound (holo) and Ca2+-free (apo) α-lactalbumin from human and bovine milk. Thermal denaturation profiles were determined from changes in the intrinsic fluorescence emission intensity (FI) as a function of temperature (T). Human apo α-lactalbumin was heat-denatured in a 2-state process with Tm = 25°C, ΔH = 167 kJ mol−1, ΔS = 7700 J mol−1 K−1 and ΔCp = 15400 J mol−1 K−1. The corresponding values for bovine apo α-lactalbumin were: Tm = 20°C, ΔH = 180 kJ mol−1, ΔS = 9000 J mol−1 K−1 and ΔCp = 5100 J mol−1 K−1. Derivative plots of d(FI)d(T) versus T revealed that both human and bovine holo α-lactalbumin were heat-denatured via a 3-state process. Thermal denaturation transitions were associated with a Tm value of 67°C or 42°C, based on changes in tryptophan or tyrosine FI results, respectively. Apparently Ca2+-bound α-lactalbumin possesses two regions (domains) with significantly different conformational stability. Based on tryptophan fluorescence measurements, ΔH = 330 kJ mol−1, ΔS = 4600 J mol−1 K−1 and ΔCp = 8200 J mol−1 K−1 for human or bovine holo α-lactalbumin. From tyrosine fluorescence emission changes, ΔH = 54–103 kJ mol−1, ΔS = 300–2000 J mol−1 K−1 and ΔCp = 3000–4000 J mol−1 K−1." @default.
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- W2040389986 date "1995-09-01" @default.
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- W2040389986 title "Thermodynamic parameters for 3-state thermal denaturation of human and bovine α-lactalbumin" @default.
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- W2040389986 doi "https://doi.org/10.1016/0040-6031(95)02292-a" @default.
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