Purification and characterization of an acid glutathione S-transferase from human lung.
Purification and characterization of an acid glutathione S-transferase from human lung.
复制标题
人肺酸性谷胱甘肽 S-转移酶的纯化和表征。
DOI：
10.3109/00365518109090515
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发表时间：
1981
影响因子：
2.1
通讯作者：
R. Tenhunen
中科院分区：
文献类型：
--
作者：
K. Koskelo;E. Valmet;R. Tenhunen
对人肺酸性谷胱甘肽S-转移酶（EC：2.5.1.18）进行了纯化和表征。纯化过程包括两个等电聚焦运行，Sephadex G-100凝胶过滤，谷胱甘肽亲和层析，Sephadex G-75凝胶过滤。关于所研究的性质，酸性肺转移酶不同于人肝转移酶α-β，但它与其他人低pI转移酶非常相似。胆红素影响肺酶的动力学显着不同，与转移酶p相比，这表明这些酶之间可能的非同一性。酸性肺转移酶约占本工作中使用的肺100，000 g上清液的总谷胱甘肽转移酶活性的97%。
An acid glutathione S-transferase (EC: 2.5.1.18) from human lung was purified and characterized. The purification procedure included two isoelectric focusing runs, Sephadex G-100 gel filtration, glutathione-affinity chromatography, and Sephadex G-75 gel filtration. With respect to the properties studied the acid lung transferase differed from human liver transferases alpha-epsilon, but it bore a close resemblance to the other human low pI transferases. Bilirubin affected the kinetics of the lung enzyme markedly differently as compared with transferase p, suggesting possible nonidentity between these enzymes. The acid lung transferase represented about 97% of the total glutathione transferase activity of the lung 100,000 g supernatant used in this work.
人肝脏谷胱甘肽 S-转移酶阴离子和阳离子形式之间的相互关系。
DOI：
10.1042/bj1910001
发表时间：
1980
期刊：
The Biochemical journal
影响因子：
--
作者：
Awasthi,YC;Dao,DD;Saneto,RP
通讯作者：
Saneto,RP