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AJP - Gastrointestinal and Liver Physiology, Vol 254, Issue 4 465-G470, Copyright © 1988 by American Physiological Society
ARTICLES |
T. Horie, T. Mizuma, S. Kasai and S. Awazu
Department of Biopharmaceutics, Tokyo College of Pharmacy, Japan.
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.
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