title: Differential scanning calorimetric studies on bovine serum albumin: I. Effects of pH and ionic strength.
abstract: Using defatted and SH-blocked bovine serum albumin (BSA), the measurement of differential scanning calorimetry (d.s.c.) was performed in the range pH 3-11 and ionic strength 0.001-1 M. The shape of the d.s.c. curve was classified into four regimes: (i) the curve with no peak, (ii) that with a peak, (iii) that with a peak having a shoulder, and (iv) that with two peaks. The presence of two peaks was interpreted by the concept of 'heat-induced transition'. The BSA molecule is composed of two domains, thermodynamically independent owing to the formation of a crevice in BSA in a particular range of pH and ionic strength; this gives two peaks in the d.s.c. curve. The enthalpy (delta H) from the d.s.c. curve was plotted against pH and against the NaCl concentration. The value of delta H increased with the increase in the ionic strength in the pH range 5.6-9.0. The temperature of thermal denaturation (the temperature of the peak maximum, Td) was raised with the increase in the ionic strength in the pH range 4.5-9.0, but was lowered in the pH range 3.5-4.0. BSA was stabilized in the neutral-alkaline pH range by the presence of NaCl, but was destabilized in the acidic pH range.
authors.affiliation: Daiichi College of Pharmaceutical Sciences, Fukuoka, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Yamasaki
authors.forename: H
authors.initials: H
authors.lastname: Yano
authors.forename: K
authors.initials: K
authors.lastname: Aoki
mesh_terms: D002152:Calorimetry, Differential Scanning; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D009994:Osmolar Concentration; D011489:Protein Denaturation; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D012710:Serum Albumin, Bovine