Effect of volatile anesthetics on the circular dichroism of bilirubin bound to human serum albumin
- 1 March 1992
- journal article
- research article
- Published by Springer Nature in Cellular and Molecular Life Sciences
- Vol. 48 (3) , 246-248
- https://doi.org/10.1007/bf01930465
Abstract
The characteristic circular dichroism of bilirubin bound to human serum albumin undergoes a remarkable sign inversion on addition of halothane, chloroform and other volatile anesthetics. This sign inversion, which is completely reversed by removal of the anesthetic, reflects a pronounced conformational change of the bound ligand; probably a complete inversion of chirality. The observation suggests that association of volatile anesthetics with proteins can markedly alter the internal topography of receptor sites and potentially influence the stereoselectivity of ligand binding.Keywords
This publication has 23 references indexed in Scilit:
- CD spectrum of bacteriorhodopsinBiophysical Journal, 1991
- Thiopental binding to human serum albumin in the presence of halothaneActa Anaesthesiologica Scandinavica, 1990
- Complementarity and chiral recognition: enantioselective complexation of bilirubinJournal of the American Chemical Society, 1987
- The interaction of enflurane, halothane and the halothane metabolite trifluoroacetic acid with the binding of acidic drugs to human serum albuminBiochemical Pharmacology, 1986
- Do general anaesthetics act by competitive binding to specific receptors?Nature, 1984
- Molecular mechanisms of general anaesthesiaNature, 1982
- The structure of triclinic bilirubin chloroform–methanol solvateActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1980
- The structure of bilirubinProceedings of the Royal Society of London. B. Biological Sciences, 1978
- Structure of bilirubinNature, 1976
- Halothane interactions with haemoglobinProceedings of the Royal Society of London. B. Biological Sciences, 1976