Nunes R, Kiang C L, Sorrentino D, Berk P D
Department of Medicine, Mount Sinai School of Medicine, City University of New York, NY 10029-1079.
J Hepatol. 1988 Dec;7(3):293-304. doi: 10.1016/s0168-8278(88)80001-1.
When freshly isolated well-stirred single cell suspensions of rat hepatocytes were incubated with 5-600 microM [3H]oleate or [35S]sulfobromophthalein (BSP) in the presence of 150 microM bovine serum albumin (BSA), uptake of both ligands increased as a linear function of the total ligand concentration in the medium. By contrast, when the same ligand concentrations were incubated as 1:1 complexes with BSA, apparent saturation of ligand uptake was observed. Analogous results were obtained in incubations employing beta-lactoglobulin instead of BSA. In none of these studies did ligand uptake velocity correlate in simple fashion with the concentration of unbound ligand in the incubation medium. These studies establish that the basis for the kinetic observations termed the 'albumin receptor phenomenon' does not require an intact hepatic lobular architecture or space of Disse, and is not specific for albumin.
当将新鲜分离的、充分搅拌的大鼠肝细胞单细胞悬液在150微摩尔牛血清白蛋白（BSA）存在的情况下与5 - 600微摩尔[³H]油酸或[³⁵S]磺溴酞钠（BSP）一起孵育时，两种配体的摄取量均随培养基中总配体浓度呈线性增加。相比之下，当相同的配体浓度以与BSA的1:1复合物形式孵育时，观察到配体摄取明显饱和。在使用β-乳球蛋白代替BSA的孵育实验中也获得了类似结果。在这些研究中，配体摄取速度均未与孵育培养基中未结合配体的浓度以简单方式相关。这些研究表明，被称为“白蛋白受体现象”的动力学观察结果的基础并不需要完整的肝小叶结构或狄氏间隙，并且对白蛋白不具有特异性。
