Scriven A J, Hume R, Nimmo I A, Strange R C
Biochim Biophys Acta. 1986 Mar 19;881(1):93-9. doi: 10.1016/0304-4165(86)90101-7.
The possibility that the GST1 phenotype of human liver cytosol is a determinant of bile salt binding has been investigated by using equilibrium dialysis and gel-exclusion chromatography. Binding of bile salts was non-saturable and whereas the glutathione S-transferases did not appear to be major bile salt binders, other binding components with molecular weights of 35 000 and 11 000 were identified in both fetal and adult cytosols.
利用平衡透析和凝胶排阻色谱法研究了人肝细胞溶质中谷胱甘肽S-转移酶1(GST1)表型作为胆汁盐结合决定因素的可能性。胆汁盐的结合是非饱和的,虽然谷胱甘肽S-转移酶似乎不是主要的胆汁盐结合蛋白,但在胎儿和成人的细胞溶质中均鉴定出分子量为35000和11000的其他结合成分。