CHARACTERIZATION OF THE INTERACTION OF ALBUMIN WITH ISOLATED RAT LIVER CELLS TO REVEAL THE MECHANISM OF ALBUMIN-MEDIATED HEPATIC TRANSPORT

Abstract

The binding of bovine serum albumin (BSA), containing ¹²⁵I-BSA, to isolated rat hepatocytes was studied over a 300-fold concentration range of BSA to characterize the interaction between albumin and the liver cells in albumin-mediated hepatic transport. The binding of BSA with a high affinity to the cell surface of hepatocytes was not found in the binding behavior. The bound fraction of BSA with hepatocytes was about 1% over those concentration range of BSA.