Karaseva E I, Eremin A N, Metelitsa D I
Prikl Biokhim Mikrobiol. 1990 May-Jun;26(3):341-8.
Thermal inactivation of glucose-6-phosphate dehydrogenase (G6PDH) and its conjugates with progesterone containing 3, 7 and 35 molecules of the modifier was studied in bidistilled water over a temperature range 35-47 degrees. At different temperatures and initial concentrations of the enzyme and its modified forms, thermal inactivation is described by the equation of the first order up to a significant degree of enzyme deactivation. The effective Kin values are decreased with the increase of the native G6PDH concentration and changed in a complicated manner with the increase of the conjugate concentration depending on the enzyme modification degree, which reflects a great role of the enzyme hydrophobicity in its inactivation. The role of hydrophobicity of the modified G6PDH in changes of its specific activity is discussed.
在双蒸水中，于35 - 47摄氏度温度范围内研究了葡萄糖-6-磷酸脱氢酶（G6PDH）及其与含有3、7和35个修饰剂分子的孕酮的缀合物的热失活情况。在不同温度以及酶及其修饰形式的初始浓度下，直至酶显著失活程度，热失活均可用一级方程描述。有效Kin值随天然G6PDH浓度的增加而降低，并随缀合物浓度的增加而以复杂方式变化，这取决于酶的修饰程度，这反映了酶的疏水性在其失活过程中起很大作用。讨论了修饰后G6PDH的疏水性在其比活性变化中的作用。
