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  Changes of the fluorescence of l-Anilino-8-naphtalenesulfonate, associated with the membranes of the sarcoplasmic reticulum, induced by general anesthetics

Augustin, J., & Hasselbach, W. (1973). Changes of the fluorescence of l-Anilino-8-naphtalenesulfonate, associated with the membranes of the sarcoplasmic reticulum, induced by general anesthetics. European Journal of Biochemistry, 39(1), 75-84. doi:10.1111/j.1432-1033.1973.tb03105.x.

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Augustin, Jan1, Author           
Hasselbach, Wilhelm2, Author           
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1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: The fluorescence of 1-anilino-8-naphthalene sulfonate (ANS), dissolved in buffer, is enhanced by the narcotics ether and halothane.

Ether and halothane considerably reduce the quantum yield of ANS, bound to native and lipid-depleted sarcoplasmic vesicles. Obviously the effect of the anesthetics takes place at the same sites before and after delipidation.

The excitation spectrum of ANS, associated with the sarcoplasmic membranes, is resolved by halothane into at least two maxima with a new separate maximum at 394 nm. The emission spectrum is not influenced.

The narcotics are only able to influence the fluorescence of those ANS molecules which can be displaced by oleic acid, a noncompetitive inhibitor of the interaction of the dye with the membranes of native and lipid-depleted vesicles.

Higher homologues of diethylether did not influence the fluorescence. Fluorescence quenching by ether and halothane is enhanced with rising temperatures. The polarisation of the fluorescence of membrane-bound ANS is enhanced by halothane.

The intrinsic fluorescence of native and lipid-depleted vesicles is considerably decreased by halothane, hardly influenced by ether. Concentrations of 2.2 M sucrose completely abolish the fluorescence quenching by the narcotics.

All effects produced by ether and halothane are reversible.

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Language(s): eng - English
 Dates: 1973-07-022005-03-031973-11
 Publication Status: Issued
 Pages: 10
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 Rev. Type: Peer
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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 39 (1) Sequence Number: - Start / End Page: 75 - 84 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040