ISSN:
1420-9071
Keywords:
Bilirubin
;
albumin
;
halothane
;
anesthesia
;
circular dichroism
;
exciton coupling
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01930465
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