'Albumin-receptor' uptake kinetics do not require an intact lobular architecture and are not specific for albumin.

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.