Homma H, Listowsky I
Biochem Biophys Res Commun. 1985 Mar 15;127(2):425-32. doi: 10.1016/s0006-291x(85)80178-9.
Anionic (Yb) rat liver glutathione-S-transferases are susceptible to temperature or pH dependent transitions to more basic forms of this class of proteins. At elevated temperatures (25-30 degrees) or at pH values above 9.0 the protein is rapidly and irreversibly converted to forms that are no longer retained by anion exchange resins and display basic components in chromatofocusing systems, because bound glutathione is removed at the higher temperatures or pH. Sharp increases in enzymatic activity with 1,2-dichloro-4-nitrobenzene as a substrate, accompany the temperature induced changes. Microheterogeneity patterns for this protein are contingent upon these interconversions, and the results explain apparent variations in relative amounts of the multiple forms under different conditions in terms of glutathione binding.
阴离子型（镱）大鼠肝脏谷胱甘肽-S-转移酶易受温度或pH值影响，转变为该类蛋白质更碱性的形式。在高温（25 - 30摄氏度）或pH值高于9.0时，蛋白质会迅速且不可逆地转化为不再被阴离子交换树脂保留的形式，并在色谱聚焦系统中显示出碱性成分，因为在较高温度或pH值下结合的谷胱甘肽会被去除。以1,2 - 二氯 - 4 - 硝基苯为底物时，酶活性会随着温度诱导的变化而急剧增加。该蛋白质的微异质性模式取决于这些相互转化，研究结果从谷胱甘肽结合的角度解释了在不同条件下多种形式相对含量的明显差异。
