Binding of glutathione by rat liver cytosol.
Binding of glutathione by rat liver cytosol.
复制标题
大鼠肝细胞质与谷胱甘肽的结合。
DOI：
10.1159/000137945
复制
发表时间：
1984
期刊：
影响因子：
3.1
通讯作者：
Kaplowitz,N
中科院分区：
文献类型：
--
作者：
Sugiyama,Y;Kaplowitz,N
Glutathione (GSH) binding to rat liver cytosol at two different protein concentrations and a range of GSH concentrations was determined using rapid ultrafiltration. Two binding sites and nonspecific binding were determined by computer fit of the data. The high-affinity site had a similar affinity and capacity for GSH as that of the GSH S-transferases. Using the converged parameters and an estimation of cytosolic protein content of the intact liver, simulation of the GSH-free fraction and the contribution and degree of saturation of the high-affinity binding site were estimated over a broad range of GSH concentrations. The findings predict that 70–75% of cytosol GSH is free and that the high-affinity site is saturated with GSH in the physiologic range.
