Alin P, Jensson H, Guthenberg C, Danielson U H, Tahir M K, Mannervik B
Anal Biochem. 1985 May 1;146(2):313-20. doi: 10.1016/0003-2697(85)90545-7.
Seven major isoenzymes of glutathione transferase with isoelectric points ranging from pH 6.9 to 10 were isolated from rat liver cytosol. The purification procedure included affinity chromatography on immobilized S-hexylglutathione followed by high-performance liquid chromatofocusing. Characteristics, such as physical properties, reactions with antibodies, specific activities with various substrates, kinetic constants, and sensitivities to a set of inhibitors, are given for discrimination and identification of the different isoenzymes. The multiple forms of the enzyme correspond to glutathione transferases 1-1, 1-2, 2-2, 3-3, 3-4, and 4-4 in the recently introduced nomenclature [W.B. Jakoby et al. (1984) Biochem. Pharmacol. 33, 2539-2540]. A seventh form appears to be a heterodimeric protein composed of subunit 3 and an as yet unidentified subunit.
从大鼠肝脏胞液中分离出了七种主要的谷胱甘肽转移酶同工酶，其等电点范围为pH 6.9至10。纯化过程包括在固定化S-己基谷胱甘肽上进行亲和层析，然后进行高效液相色谱聚焦。给出了诸如物理性质、与抗体的反应、对各种底物的比活性、动力学常数以及对一组抑制剂的敏感性等特征，用于区分和鉴定不同的同工酶。在最近引入的命名法中，该酶的多种形式对应于谷胱甘肽转移酶1-1、1-2、2-2、3-3、3-4和4-4 [W.B. 雅各比等人（1984年），《生物化学与药理学》33卷，2539 - 2540页]。第七种形式似乎是一种由亚基3和一个尚未鉴定的亚基组成的异二聚体蛋白。
