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采用利用内源荧光、1-苯氨基萘-8-磺酸(ANS)荧光、酶活性的测定以及动力学分析等手段，研究肌酸激酶在氧化型的二硫基苏糖醇(DTT)溶液中的结构与活性的变化.结果表明：随着氧化型DTT浓度的增加，肌酸激酶的活性逐渐丧失，直至完全失活，并伴随着构象的变化.肌酸激酶起初微小的结构变化就会导致酶活性的迅速丧失，而且其的失活先于明显可测的整体构象变化，酶分子的活性部位处于柔性区域内.另外，随着氧化型DTT浓度的提高，肌酸激酶的内源荧光发射峰位明显地红移，外源ANS荧光强度显著增强，即酶分子的疏水面加大，该结果暗示了酶蛋白的构象发生了改变.动力学分析表明，氧化型DTT对肌酸激酶的氧化过程是一个慢的可逆抑制过程，其反应的表观速率常数A的大小与氧化型DTT的浓度无关，因此是非络合型的.

利用内源荧光、1-苯氨基萘-8-磺酸(ANS)荧光、远紫外-圆二色光谱以及酶活力测定等手段研究了精氨酸激酶在1，1，1，3，3，3-六氟异丙醇(HFIP)溶液中变性后结构与活性的变化.为避免蛋白质聚沉的出现，实验中采用的变性剂浓度低于8%.当六氟异丙醇浓度为0.5%~1.5%时，蛋白质的二级结构和内源荧光发射峰位都没有发生明显的变化，而外源ANS荧光强度则显著增强.继续提高变性剂浓度至6%后，内源荧光发射峰位明显红移、二级结构含量增大、外源荧光减弱、酶活力完全丧失.内源荧光和外源ANS荧光的变化证明：在0.5%~1.5%六氟异丙醇浓度范围内，蛋白质分子以一种结构相对稳定并类似于天然蛋白结构的熔球态中间体的状态存在.这种熔球态中间体也是精氨酸激酶在去折叠过程中出现的一个平衡态中间体.

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