Conformational change in plasma albumin due to interaction with isolated rat hepatocyte.
The electron spin resonance spectroscopy of 4-isothiocyanato-tempo labeled to bovine serum albumin (BSA) and the absorption spectroscopy of eosin maleimide labeled to BSA in the isolated rat hepatocyte suspension indicate conformational change occurring in the albumin molecule during interaction with the hepatocellular membrane. The conformational change in the albumin molecule may possibly accelerate the dissociation of albumin-organic anion complexes at the surface of the liver cell. The conformational change in the albumin molecule may explain in part the mechanism of albumin-mediated hepatic transport.
Horie
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Department of Biopharmaceutics, Tokyo College of Pharmacy, Japan.
Mizuma
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Kasai
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Awazu
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D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D002478:Cells, Cultured; D003497:Cyclic N-Oxides; D004578:Electron Spin Resonance Spectroscopy; D004910:Erythrocyte Membrane / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism; D008099:Liver / Q000378:metabolism*; D008297:Male; D008954:Models, Biological; D011487:Protein Conformation; D051381:Rats; D011919:Rats, Inbred Strains; D012710:Serum Albumin, Bovine / Q000378:metabolism*
D003497:Cyclic N-Oxides; D012710:Serum Albumin, Bovine; C003959:TEMPO