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Journal of Lipid Research, Vol. 46, 1755-1764, August 2005
Copyright © 2005 by American Society for Biochemistry and Molecular Biology
Max-Planck-Institut für Biochemie, 82152 Martinsried, Germany
Published, JLR Papers in Press, June 1, 2005. DOI 10.1194/jlr.M500138-JLR200
1 To whom correspondence should be addressed. e-mail: renner{at}biochem.mpg.de
In the purple membrane (PM) of halobacteria, lipids stabilize the trimeric arrangement of bacteriorhodopsin (BR) molecules and mediate the packing of the trimers in a regular crystalline arrangement. To date, the identification and quantification of these lipids has been based either on lipid extraction procedures or structural models. By directly solubilizing PMs from Halobacterium salinarum in aqueous detergent solutions (SDS or Triton X-100), we avoided any separation or modification steps that might modify the lipid composition or even the lipid molecules themselves. Our analysis of integral PM preparations should resolve partially conflicting literature data on the lipid composition of the PM. Using 31P and 1H NMR of detergent-solubilized but otherwise untreated samples, we found two glycolipids and 6.4 ± 0.1 phospholipids per BR molecule, 4.4 ± 0.1 of the latter being the phosphatidylglycerophosphate methyl ester. The only glycolipid detected was S-TGD-1.
For an additional glycolipid, glycocardiolipin, that was recently identified in lipid extracts, we show that it was produced mainly during the lipid extraction procedure but also was partially dependent on the preparation of the PM suspensions.
Supplementary key words phospholipids glycolipids nuclear magnetic resonance bacteriorhodopsin
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