PMID: 9630603Jun 19, 1998Paper

Selectivity of lipid-protein interactions with trypsinized Na, K-ATPase studied by spin-label EPR

Biochimica Et Biophysica Acta
Ashish AroraDerek Marsh

Abstract

The selectivity of the lipid-protein interactions in trypsinised Na, K-ATPase membranes from Squalus acanthias has been determined by using EPR spectroscopy with different lipid probes spin-labelled on the 14-C atom of the fatty acid chain. From measurements at low ionic strength and different pH values, the pattern of selectivity is: (stearic acid)->(phosphatidylserine)->(stearic acid)0>(phosphatidylcholine)+/-, where superscripts indicate the formal electrostatic charge on the lipid headgroup. This is in the same order as that determined with native Na,K-ATPase membranes [M. Esmann, D. Marsh, Biochemistry 24 (1985) 3572-3578]. The selectivity for phosphatidylserine is independent of pH, over the range pH 6.0-9. 0, as found also for native membranes. For membranes trypsinised in the presence of Rb+ ions, and in the presence of Na+ (which allows more extensive proteolysis), the relative association constants, Kr, of all lipids are the same as for control membranes, with the exception of ionised (stearic acid)- that shows the highest specificity. Therefore, both the stoichiometry and the principal determinants of the specificity of lipid-protein interaction are preserved on extensive trypsinisation of Na,K-ATPase membranes. This...Continue Reading

References

Jul 27, 1992·Biochimica Et Biophysica Acta·M Esmann, L Sottrup-Jensen
Jun 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·S J KarlishW D Stein
Sep 1, 1981·Biochemistry·J R BrotherusL E Hokin

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Citations

Feb 26, 2008·Biochimica Et Biophysica Acta·Derek Marsh
Apr 4, 2006·Chemistry and Physics of Lipids·Mikael Esmann, Derek Marsh
Aug 2, 2008·Methods : a Companion to Methods in Enzymology·Derek Marsh

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