Lyubarev A E, Kurganov B I, Orlov V N, Zhou H M
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia.
Biophys Chem. 1999 Jun 28;79(3):199-204. doi: 10.1016/s0301-4622(99)00050-2.
Thermal denaturation of creatine kinase from rabbit skeletal muscle has been studied by differential scanning calorimetry. The excess heat capacity vs. temperature profiles were independent of protein concentration, but strongly temperature scanning rate-dependent. It has been shown that thermal denaturation of creatine kinase satisfies the previously proposed validity criteria for the two-state irreversible model [Kurganov et al., Biophys. Chem.70 (1997) 125]. The energy activation value has been calculated to be 461.0 +/- 0.7 kJ/mol.
通过差示扫描量热法研究了兔骨骼肌肌酸激酶的热变性。过量热容量与温度的关系曲线与蛋白质浓度无关，但强烈依赖于温度扫描速率。结果表明，肌酸激酶的热变性符合先前提出的两态不可逆模型的有效性标准[库尔加诺夫等人，生物物理化学杂志70 (1997) 125]。计算出的能量活化值为461.0 +/- 0.7 kJ/mol。
