Sugiyama Y, Kaplowitz N
Pharmacology. 1984;28(2):61-6. doi: 10.1159/000137945.
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.
利用快速超滤法测定了谷胱甘肽（GSH）在两种不同蛋白质浓度以及一系列GSH浓度下与大鼠肝脏胞质溶胶的结合情况。通过对数据进行计算机拟合确定了两个结合位点和非特异性结合。高亲和力位点对GSH的亲和力和结合能力与谷胱甘肽S-转移酶相似。利用收敛参数以及对完整肝脏胞质溶胶蛋白质含量的估算，在广泛的GSH浓度范围内估算了无GSH组分、高亲和力结合位点的贡献及饱和程度。研究结果预测，70 - 75%的胞质溶胶GSH是游离的，且在生理范围内高亲和力位点被GSH饱和。
