Spectroscopic analysis of halothane binding to the plasma membrane Ca2+-ATPase

Biophysical Journal
M M Lopez, D Kosk-Kosicka

Abstract

The intrinsic tryptophan (Trp) fluorescence of the plasma membrane Ca2+-ATPase (PMCA) is significantly quenched by halothane, a volatile anesthetic common in clinical practice. It has been proposed that halothane inhibition of the Ca2+-ATPase activity results from conformational changes following anesthetic binding in the enzyme. We have investigated whether the observed quenching reflects halothane binding to PMCA. We have shown that the quenching is dose dependent and saturable and can be fitted to a binding curve with an equilibrium constant K(Hal) = 2.1 mM, a concentration at which the anesthetic approximately half-maximally inhibits the Ca2+-ATPase activity. The relatively low sensitivity of halothane quenching of Trp fluorescence to the concentration of phosphatidylcholine and detergent in the PMCA preparation concurs with the quenching resulting from anesthetic binding in the PMCA molecule. Analysis of the Trp fluorescence quenching by acrylamide indicates that the Trp residues are not considerably exposed to the solvent (Stern-Volmer quenching constant of 2.9 M(-1)) and do not differ significantly in their accessibility to halothane. Other volatile anesthetics, diethyl ether and diisopropyl ether, reduce the quenching c...Continue Reading

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Citations

Jun 13, 2009·International Journal of Biological Sciences·Aili WangQinyi Zhao
Aug 1, 2006·Biophysical Journal·John H StreiffKeith A Jones
May 11, 2001·The Journal of Biological Chemistry·M J BecksteadS J Mihic
Dec 22, 2009·ACS Nano·Silvia H De Paoli LacerdaJack F Douglas
Aug 14, 2002·British Journal of Anaesthesia·M J Rebecchi, S N Pentyala
Jan 25, 2018·Langmuir : the ACS Journal of Surfaces and Colloids·Ramón RialJuan M Ruso
Jul 17, 1999·Analytical Chemistry·C K LariveS Bogdanowich-Knipp
Oct 13, 2009·Archives of Biochemistry and Biophysics·Miguel R Lugo, Frances J Sharom

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