The isozyme pattern of glutathione S‐transferases in rat heart
The isozyme pattern of glutathione S‐transferases in rat heart
复制标题
大鼠心脏谷胱甘肽S-转移酶同工酶模式
DOI：
10.1016/0014-5793(84)80309-9
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发表时间：
1984
期刊：
影响因子：
3.5
通讯作者：
H. Sies
中科院分区：
文献类型：
--
作者：
T. Ishikawa;H. Sies
大鼠心脏谷胱甘肽转移酶同工酶谱与肝脏有显著差异。心脏缺乏大鼠肝脏识别的大部分碱性同工酶，通过亲和层析获得的谷胱甘肽-转移酶对-己基谷胱甘肽连接的Sepharose 6B的等电集中显示，心脏中存在3种主要的酸性同工酶，pi值分别为6.8、6.3和4.9，其中至少有两种在肝脏中未发现。此外，谷胱甘肽转移酶活性和蛋白染色在5.0-5.5的pIrange中发现多个条带。
The isozyme pattern of glutathioneS-transferases of rat heart differs markedly from that of liver. Heart lacks the majority of basic isozymes recognized in rat liver, and isoelectric focusing of glutathioneS-transferases obtained from affinity chromatography onS-hexylglutathione-linked Sepharose 6B revealed that 3 major acidic isozymes with pIvalues of 6.8, 6.3 and 4.9 are present in heart, at least two of which were not found in liver. In addition, multiple bands were found in the pIrange 5.0–5.5 for glutathioneS-transferase activity and protein staining.
大鼠谷胱甘肽 S-转移酶的组织特异性表达。
DOI：
--
发表时间：
1983
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Tu,CP;Weiss,MJ;Li,NQ;Reddy,CC
通讯作者：
Reddy,CC