Characterization of the interaction of albumin with isolated rat liver cells to reveal the mechanism of albumin-mediated hepatic transport.
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.
D000818:Animals; D001692:Biological Transport; D003911:Dextrans / Q000378:metabolism; D066298:In Vitro Techniques; D008099:Liver / Q000378:metabolism*; D008297:Male; D011485:Protein Binding; D051381:Rats; D011919:Rats, Inbred Strains; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013448:Sulfobromophthalein / Q000378:metabolism
D003911:Dextrans; D013448:Sulfobromophthalein; D012710:Serum Albumin, Bovine