Tateoka N, Tsuchida S, Soma Y, Sato K
Clin Chim Acta. 1987 Jul 15;166(2-3):207-18. doi: 10.1016/0009-8981(87)90423-2.
Four glutathione S-transferase (GST, EC 2.5.1.18) forms were purified from human kidney by S-hexylglutathione affinity chromatography followed by chromatofocusing using a fast protein liquid chromatography system. These forms were demonstrated to be identical with GSTs I, II, IV, V(pi) in human liver previously characterized by us, by SDS-polyacrylamide slab gel electrophoresis, two-dimensional gel electrophoresis and double immunodiffusion. GST III (mu) was not detected in any of 5 specimens examined. GST-pi was a major form in the kidney. The activity was 30-40% of the total activity in kidney cytosol and the protein amount was approximately 140 micrograms/g of tissue; 0.27% of the total cytosol protein amount. In many organs including the placenta, GST-pi is present at levels similar to that in the kidney but low in the liver (34 micrograms/g).
通过S-己基谷胱甘肽亲和层析，随后使用快速蛋白质液相色谱系统进行色谱聚焦，从人肾中纯化出四种谷胱甘肽S-转移酶（GST，EC 2.5.1.18）形式。通过SDS-聚丙烯酰胺平板凝胶电泳、二维凝胶电泳和双向免疫扩散证明，这些形式与我们之前在人肝脏中鉴定的GSTs I、II、IV、V（pi）相同。在所检测的5个样本中均未检测到GST III（mu）。GST-pi是肾脏中的主要形式。其活性占肾细胞溶质总活性的30-40%，蛋白质含量约为140微克/克组织；占细胞溶质总蛋白质含量的0.27%。在包括胎盘在内的许多器官中，GST-pi的含量与肾脏中的相似，但在肝脏中含量较低（34微克/克）。
