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1986•Journal of Pharmacobio-DynamicsOpen access

Characterization of the interaction of albumin with isolated rat liver cells to reveal the mechanism of albumin-mediated hepatic transport.

Takashi Mizuma, Toshiharu Horie, Masahiro Hayashi, Shoji Awazu

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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.

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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.

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Available 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.

Key concepts: Bovine serum albumin, Albumin, Hepatocyte, Chemistry, Serum albumin, Biochemistry, Plasma protein binding, In vitro

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Characterization of the interaction of albumin with isolated rat liver cells to reveal the mechanism of albumin-mediated hepatic transport. — Research Paper | ScholarLens