尿苷二磷酸葡萄糖醛酸基转移酶的磷脂依赖性。微粒体酶活性的温度依赖性（逆反应）。
The phospholipid-dependence of uridine diphosphate glucuronyltransferase. Temperature-dependence of microsomal enzyme activity (reverse reaction).
作者信息
Cummings J, Graham A B, Wood G C
出版信息
Biochem J. 1980 Feb 1;185(2):521-6. doi: 10.1042/bj1850521.
Arrhenius plots of the non-latent UDP-glucuronlytransferase reverse reaction (p-nitrophenyl glucuronide donor) activity of guinea-pig microsomal membranes prepared with 15 mM-KCl were linear from 5 to 40 degrees C. These plots for other preparations from guinea-pig and rat liver (i.e. preparations that show transferase latency) exhibited two linear regions intersecting at a transition point near 19--21 degrees C. This discontinuity was abolished when latency was removed by treating the membranes with perturbants of phospholipid-bilayer structure. Thus the temperature-depdendnces of the reverse reaction catalysed by the enzymes of these various preparations are similar to those of the corresponding forward reactions [Pechey, Graham & Wood (1978) Biochem. J. 175, 115--1124]. Perturbants activated the enzyme of KCl-prepared guinea-pig microsomal membranes only slightly and caused no significant alteration to Arrhenius plots of its forward or reverse reaction activities. These results support the 'compartmentation' theory of UDP-glucuronyltransferase lactency.
用15 mM - KCl制备的豚鼠微粒体膜的非潜伏性UDP - 葡糖醛酸基转移酶逆反应（对硝基苯基葡糖醛酸供体）活性的阿伦尼乌斯曲线在5至40摄氏度范围内呈线性。豚鼠和大鼠肝脏的其他制剂（即显示转移酶潜伏性的制剂）的这些曲线在接近19 - 21摄氏度的转变点处呈现出两个相交的线性区域。当用磷脂双层结构的扰动剂处理膜以消除潜伏性时，这种不连续性就消失了。因此，这些不同制剂的酶催化的逆反应的温度依赖性与相应的正向反应相似[佩奇、格雷厄姆和伍德（1978年）《生物化学杂志》175卷，115 - 1124页]。扰动剂仅轻微激活了用KCl制备的豚鼠微粒体膜的酶，并且对其正向或逆反应活性的阿伦尼乌斯曲线没有显著改变。这些结果支持了UDP - 葡糖醛酸基转移酶潜伏性的“区室化”理论。
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