Juronen E, Tasa G, Uusküla M, Pooga M, Mikelsaar A V
University of Tartu, Department of Human Biology and Genetics, Estonia.
Biochem Mol Biol Int. 1996 May;39(1):21-9. doi: 10.1080/15216549600201021.
A high activity glutathione S-transferase T1-1 (GSTT1-1) towards dichloromethane was isolated from human liver cytosol and purified to homogenity in 18.5% yield with a purification factor of 4400-fold. The GSTT1-1 was also isolated from erythrocytes, but the enzyme activity decreased rapidly in the final stages of purification. The purified GSTT1-1-s were homo-dimeric enzymes with a subunit M1 value 25,300 and pI 6 64, as confirmed by SDS-PAGE, IEF and Western blot analysis. The N-terminal amino acid sequences of GSTT1-1 from liver and red blood cells, analyzed up to the 12th amino acid, were identical. Immunoblot analysis revealed that GSTT1-1 was also present in lung, kidney, brain, skeletal muscle, heart, small intestine and spleen, but not in lymphocytes.
从人肝细胞溶胶中分离出一种对二氯甲烷具有高活性的谷胱甘肽S-转移酶T1-1（GSTT1-1），并将其纯化至同质，产率为18.5%，纯化倍数为4400倍。GSTT1-1也从红细胞中分离得到，但在纯化的最后阶段酶活性迅速下降。经SDS-PAGE、IEF和蛋白质印迹分析证实，纯化的GSTT1-1是同二聚体酶，亚基M1值为25300，pI为6.64。对肝脏和红细胞中GSTT1-1的N端氨基酸序列分析至第12个氨基酸，结果相同。免疫印迹分析显示，GSTT1-1也存在于肺、肾、脑、骨骼肌、心脏、小肠和脾脏中，但不存在于淋巴细胞中。
