Abstract
As the roles of phospholipids continue to be unraveled in an expansive list of biological processes, the availability of fast, accurate, and precise analytical approaches becomes of utmost relevance. Traditional methods rely on the separation of phospholipid classes, each with a different polar head group, by either thin-layer or liquid chromatography. The length and degree of unsaturation of the hydrophobic chains are subsequently determined by derivatization and gas chromatography. Although these methods are well developed, they are time-consuming and do not allow for in situ analysis.
The combination of P-31 nuclear magnetic resonance (NMR) spectroscopy and mass spectrometry (MS) provides a powerful alternative for the analysis of phospholipids in complex mixtures. With the use of P-31 NMR spectroscopy, phospholipids can be analyzed quantitatively in either organic solvents or aqueous media containing a detergent. Matrix-assisted laser desorption/ionization (MALDI) and other forms of ionization such as electron-spray ionization (ESI) coupled with mass spectrometry (MS) allow the analysis of intact lipids both in vitro and in situ.
This chapter describes conventional approaches for phospholipid analysis first. The criteria and current options in the choice of matrices for MALDI MS are addressed. The ability of MALDI MS to image phospholipids is then highlighted as well as the remaining challenges. Regarding P-31 NMR, current studies on the measurement of temperature coefficients and pH dependences to improve the accuracy in the assignment of P-31 resonances are described. Finally, the complementary nature of P-31 NMR and MALDI MS is illustrated in the reevaluation of the unusual composition of phospholipids in human lens membranes.
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References
Gennis R. Biomembranes: molecular structure and function. New York: Springer; 1989.
Voet D, Voet JG. Biochemistry. 2nd ed. New York: Wiley & Sons; 1995. p. 1288–90.
Brites P, Waterham HR, Wanders RJA. Functions and biosynthesis of plasmalogens in health and disease. Biochim Biophys Acta. 2004;1636(2–3):219–31.
Brosche T, Platt D. Mini-review—the biological significance of plasmalogens in defense against oxidative damage. Exp Gerontol. 1998;33(5):363–9.
Garg ML, Haerdi JC. The biosynthesis and functions of plasmalogens. J Clin Biochem Nutr. 1993;14(2):71–82.
Zimmerman GA, et al. The platelet-activating factor signaling system and its regulators in syndromes of inflammation and thrombosis. Crit Care Med. 2002;30(5):S294–301.
Kulikov VI, Muzya GI. Ether lipids and platelet-activating factor: evolution and cellular function. Biochemistry (Mosc). 1997;62(10):1103–8.
Greiner JV, et al. Phospholipids in meibomian gland secretion. Ophthalmic Res. 1996;28(1):44–9.
Byrdwell WC, et al. Separation and characterization of the unknown phospholipid in human lens membranes. Invest Ophthalmol Vis Sci. 1994;35(13):4333–43.
Ferguson SR, Borchman D, Yappert MC. Confirmation of the identity of the major phospholipid in human lens membranes. Invest Ophthalmol Vis Sci. 1996;37(8):1703–6.
Kok JW, et al. Dihydroceramide biology. Structure-specific metabolism and intracellular localization. J Biol Chem. 1997;272(34):21128–36.
Folch J, Lees M, Sloane Stanley G. A simple method for the isolation and purification of total lipids from animal tissues. J Biol Chem. 1957;226:497–509.
Byrdwell WC, et al. 31P NMR quantification and monophasic solvent purification of human and bovine lens phospholipids. Lipids. 2002;37(11):1087–92.
Christie WW. Lipid analysis. 3rd ed. Bridgwater: Oily Press; 2003.
Christie WW. Separation of phospholipid classes by high-performance liquid chromatography. In: Christie WW, editor. Advances in lipid methodology—three. Dundee: Oily Press; 1996. p. 77–107.
Christie WW. The lipid library; 2007. http://www.lipidlibrary.co.uk/topics/hplc_pl/index.htm
Broekhuyse RM. Lipids in tissues of the eye. IV. Influence of age and species differences on the phospholipid composition of the lens. Biochim Biophys Acta. 1970;218(3):546–8.
Bloemendal H, et al. The plasma membranes of eye lens fibres. Biochemical and structural characterization. Cell Differ. 1972;1(2):91–106.
Merchant TE, et al. Human crystalline lens phospholipid analysis with age. Invest Ophthalmol Vis Sci. 1991;32(3):549–55.
Christie WW. Recent developments in high-performance liquid and gas-chromatography of lipids. Rev Franc Corps Gras. 1991;38(5–6):155–60.
Christie WW. A stable silver-loaded column for the separation of lipids by high-performance liquid-chromatography. J High Res Chromatogr Chromatogr Commun. 1987;10(3):148–50.
Olsson NU, Salem N. Molecular species analysis of phospholipids. J Chromatogr B. 1997;692(2):245–56.
Hutchins PM, Barkley RM, Murphy RC. Separation of cellular nonpolar neutral lipids by normal-phase chromatography and analysis by electrospray ionization mass spectrometry. J Lipid Res. 2008;49(4):804–13.
Whitehead SN, et al. Identification and quantitation of changes in the platelet activating factor family of glycerophospholipids over the course of neuronal differentiation by high-performance liquid chromatography electrospray ionization tandem mass spectrometry. Anal Chem. 2007;79(22):8539–48.
Pacetti D, et al. High performance liquid chromatography-tandem mass spectrometry of phospholipid molecular species in eggs from hens fed diets enriched in seal blubber oil. J Chromatogr A. 2005;1097(1–2):66–73.
Beermann C, et al. sn-position determination of phospholipid-linked fatty acids derived from erythrocytes by liquid chromatography electrospray ionization ion-trap mass spectrometry. Lipids. 2005;40(2):211–8.
Byrdwell WC. Dual parallel liquid chromatography/dual mass spectrometry (LC2/MS2) of bovine brain total lipid extract. J Liq Chromatogr R T. 2003;26(19):3147–81.
Kakela R, Somerharju P, Tyynela J. Analysis of phospholipid molecular species in brains from patients with infantile and juvenile neuronal-ceroid lipofuscinosis using liquid chromatography-electrospray ionization mass spectrometry. J Neurochem. 2003;84(5):1051–65.
Hallgren B, Ryhage R, Stenhagen E. The mass spectra of methyl oleate, methyl linoleate and methyl linolenate. Acta Chem Scand. 1959;13:845–7.
Karas M, et al. Laser desorption ionization mass-spectrometry of proteins of mass 100 000 to 250 000 dalton. Angew Chem Int Ed. 1989;28(6):760–1.
Hunt AN, et al. Highly saturated endonuclear phosphatidylcholine is synthesized in situ and colocated with CDP-choline pathway enzymes. J Biol Chem. 2001;276(11):8492–9.
Hunt AN, et al. Lipidomic analysis of the molecular specificity of a cholinephosphotransferase in situ. Biochem Soc Trans. 2004;32:1060–2.
Hunt AN, et al. Use of mass spectrometry-based lipidomics to probe PITP alpha (phosphatidylinositol transfer protein alpha) function inside the nuclei of PITP alpha(+/+) and PITP alpha(−/−) cells. Biochem Soc Trans. 2004;32:1063–5.
Burdge GC, Postle AD. Selective changes to phosphatidylcholine and phosphatidylethanolamine molecular species in the developing fetal guinea pig liver and plasma. Reprod Nutr Dev. 2004;44(6):571–82.
Han X, et al. Toward fingerprinting cellular lipidomes directly from biological samples by two-dimensional electrospray ionization mass spectrometry. Anal Biochem. 2004;330(2):317–31.
Takats Z, et al. Mass spectrometry sampling under ambient conditions with desorption electrospray ionization. Science. 2004;306(5695):471–3.
Jackson AU, et al. Salt tolerance of desorption electrospray ionization (DESI). J Am Soc Mass Spectrom. 2007;18:2218–25.
Cotte-Rodriguez I, Mulligan CC, Cooks G. Non-proximate detection of small and large molecules by desorption electrospray ionization and desorption atmospheric pressure chemical ionization mass spectrometry: instrumentation and applications in forensics, chemistry, and biology. Anal Chem. 2007;79(18):7069–77.
Ifa DR, et al. Development of capabilities for imaging mass spectrometry under ambient conditions with desorption electrospray ionization (DESI). Int J Mass Spectrom. 2007;259(1–3):8–15.
Wiseman JM, et al. Tissue imaging at atmospheric pressure using desorption electrospray ionization (DESI) mass spectrometry. Angew Chem Int Ed. 2006;45(43):7188–92.
Wiseman JM, et al. Mass spectrometric profiling of intact biological tissue by using desorption electrospray ionization. Angew Chem Int Ed. 2005;44(43):7094–7.
Manicke NE, et al. Desorption electrospray ionization (DESI) mass spectrometry and tandem mass spectrometry (MS/MS) of phospholipids and sphingolipids: Ionization, adduct formation, and fragmentation. J Am Soc Mass Spectrom. 2008;19(4):531–43.
Wiseman JM, et al. Ambient molecular imaging by desorption electrospray ionization mass spectrometry. Nat Protoc. 2008;3(3):517–24.
Karas M, et al. Ultraviolet-laser desorption ionization mass-spectrometry of femtomolar amounts of large proteins. Biomed Environ Mass Spectrom. 1989;18(9):841–3.
Karas M, Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10000 daltons. Anal Chem. 1988;60(20):2299–301.
Karas M, et al. Matrix-assisted ultraviolet-laser desorption of nonvolatile compounds. Int J Mass Spectrom Ion Process. 1987;78:53–68.
Karas M, Bachmann D, Hillenkamp F. Influence of the wavelength in high-irradiance ultraviolet-laser desorption mass-spectrometry of organic-molecules. Anal Chem. 1985;57(14):2935–9.
Beavis RC. Matrix-assisted ultraviolet-laser desorption—evolution and principles. Org Mass Spectrom. 1992;27(6):653–9.
Beavis RC. Phenomenological models for matrix-assisted laser desorption ion yields near the threshold fluence. Org Mass Spectrom. 1992;27(8):864–8.
Cotter RJ. Time-of-flight mass-spectrometry—basic principles and current state. Time Flight Mass Spectrom. 1994;549:16–48.
Cotter RJ. Time-of-flight mass-spectrometry for the structural—analysis of biological molecules. Anal Chem. 1992;64(21):A1027–39.
Cotter RJ. Time-of-flight mass-spectrometry—an increasing role in the life sciences. Biomed Environ Mass Spectrom. 1989;18(8):513–32.
Cotter RJ. The new time-of-flight mass spectrometry. Anal Chem. 1999;71(13):445A–51.
Tabet JC, Cotter RJ. Time-Resolved laser desorption mass-spectrometry. 2. Measurement of the energy spread of laser desorbed ions. Int J Mass Spectrom Ion Process. 1983;54(1–2):151–8.
Mamyrin BA. Time-of-flight mass spectrometry (concepts, achievements, and prospects). Int J Mass Spectrom. 2001;206(3):251–66.
Mamyrin BA. Laser-assisted reflectron time-of-flight mass-spectrometry. Int J Mass Spectrom Ion Process. 1994;131:1–19.
Ivanov MA, et al. Mass-reflectron for the study of laser irradiation interaction processes with molecules in an ultrasonic gas-jet. Zh Tekh Fiz. 1983;53(10):2039–44.
Mamyrin BA, et al. Mass-reflectron a new nonmagnetic time-of-flight high-resolution mass-spectrometer. Zh Eksp Teor Fiz. 1973;64(1):82–9.
Cotter RJ, Iltchenko S, Wang DX. The curved-field reflectron: PSD and CID without scanning, stepping or lifting. Int J Mass Spectrom. 2005;240(3):169–82.
Marto JA, et al. Structural characterization of phospholipids by matrix-assisted laser desorption/ionization Fourier transform ion cyclotron resonance mass spectrometry. Anal Chem. 1995;67(21):3979–84.
Harvey DJ. Matrix-assisted laser-desorption ionization mass-spectrometry of sphingo-lipids and glycosphingo-lipids. J Mass Spectrom. 1995;30(9):1311–24.
Solouki T, et al. Attomole biomolecule mass analysis by matrix-assisted laser desorption/ionization Fourier transform ion cyclotron resonance. Anal Chem. 1995;67(22):4139–44.
Schiller J, et al. Lipid analysis by matrix-assisted laser desorption and ionization mass spectrometry: a methodological approach. Anal Biochem. 1999;267(1):46–56.
Petkovic M, et al. The signal-to-noise ratio as the measure for the quantification of lysophospholipids by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. Analyst. 2001;126(7):1042–50.
Benard S, et al. Experiments towards quantification of saturated and polyunsaturated diacylglycerols by matrix-assisted laser desorption and ionization time-of-flight mass spectrometry. Chem Phys Lipids. 1999;100(1–2): 115–25.
Estrada R, Yappert MC. Alternative approaches for the detection of various phospholipid classes by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J Mass Spectrom. 2004;39:412–22.
Schiller J, et al. CsCl as an auxiliary reagent for the analysis of phosphatidylcholine mixtures by matrix-assisted laser desorption and ionization time-of-flight mass spectrometry (MALDI-TOF MS). Chem Phys Lipids. 2001;113(1–2):123–31.
Estrada R, Yappert MC. Regional phospholipid analysis of porcine lens membranes by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J Mass Spectrom. 2004;39(12):1531–40.
Fitzgerald MC, Parr GR, Smith LM. Basic matrices for the matrix-assisted laser-desorption ionization mass-spectrometry of proteins and oligonucleotides. Anal Chem. 1993;65(22):3204–11.
Schiller J, et al. Recent applications of MALDI-TOF mass spectrometry and P-31 NMR spectroscopy in phospholipid research. Future Lipidol. 2007;1(1):115–25.
Lorkiewicz PK, Yappert MC. 2-(2-aminoethylamino)-5-nitropyridine (AAN) as a basic matrix for negative mode matrix-assisted laser desorption/ionization of phospholipids. J Mass Spectrom. 2009;44(1):137–43.
Oborina EM, Yappert MC. Effect of sphingomyelin versus dipalmitoylphosphatidylcholine on the extent of lipid oxidation. Chem Phys Lipids. 2003;123:223–32.
Rujoi M, et al. Isolation and lipid characterization of cholesterol-enriched fractions in cortical and nuclear human lens fibers. Invest Ophthalmol Vis Sci. 2003;44(4):1634–42.
Caprioli RM, Farmer TB, Gile J. Molecular imaging of biological samples: localization of peptides and proteins using MALDI-TOF MS. Anal Chem. 1997;69(23):4751–60.
Chaurand P, Stoeckli M, Caprioli RM. Direct profiling of proteins in biological tissue sections by MALDI mass spectrometry. Anal Chem. 1999;71(23):5263–70.
Stoeckli M, et al. Imaging mass spectrometry: a new technology for the analysis of protein expression in mammalian tissues. Nat Med. 2001;7(4):493–6.
Chaurand P, Caprioli RM. Direct profiling and imaging of peptides and proteins from mammalian cells and tissue sections by mass spectrometry. Electrophoresis. 2002;23(18):3125–35.
Brunelle A, Laprevote O. Recent advances in biological tissue Imaging with time-of-flight secondary ion mass spectrometry: polyatomic ion sources, sample preparation, and applications. Curr Pharm Des. 2007;13(32):3335–43.
Sjovall P, et al. Imaging of membrane lipids in single cells by imprint-imaging time-of-flight secondary ion mass spectrometry. Anal Chem. 2003;75(14):3429–34.
Yappert MC, Borchman D. Sphingolipids in human lens membranes: an update on their composition and possible biological implications. Chem Phys Lipids. 2004;129:1–20.
Yappert MC, et al. Glycero- versus sphingo-phospholipids: correlations with human and non-human mammalian lens growth. Exp Eye Res. 2003;76(6):725–34.
Rujoi M, Estrada R, Yappert MC. In situ MALDI-TOF MS regional analysis of neutral phospholipids in lens tissue. Anal Chem. 2004;76(6):1657–63.
Shimma S, et al. MALDI-based imaging mass spectrometry revealed abnormal distribution of phospholipids in colon cancer liver metastasis. J Chromatogr B Analyt Technol Biomed Life Sci. 2007;855(1):98–103.
Herring KD, Oppenheimer SR, Caprioli RM. Direct tissue analysis by matrix-assisted laser desorption ionization mass spectrometry: application to kidney biology. Semin Nephrol. 2007;27(6):597–608.
Jackson SN, et al. MALDI-ion mobility-TOFMS imaging of lipids in rat brain tissue. J Mass Spectrom. 2007;42(8):1093–8.
McLean JA, Ridenour WB, Caprioli RM. Profiling and imaging of tissues by imaging ion mobility-mass spectrometry. J Mass Spectrom. 2007;42(8):1099–105.
Jackson SN, Wang HYJ, Woods AS. In situ structural characterization of glycerophospholipids and sulfatides in brain tissue using MALDI-MS/MS. J Am Soc Mass Spectrom. 2007;18(1):17–26.
Woods AS, Jackson SN. Brain tissue lipidomics: direct probing using matrix-assisted laser desorption/ionization mass spectrometry. AAPS J. 2006;8(2):E391–5.
Jones JJ, et al. Characterizing the phospholipid profiles in mammalian tissues by MALDI FTMS. Anal Chem. 2006;78(9):3062–71.
Jackson SN, Wang HYJ, Woods AS. In situ structural characterization of phosphatidylcholines in brain tissue using MALDI-MS/MS. J Am Soc Mass Spectrom. 2005;16(12):2052–6.
Jackson SN, Wang HYJ, Woods AS. Direct profiling of lipid distribution in brain tissue using MALDI-TOFMS. Anal Chem. 2005;77(14):4523–7.
Jackson SN, Wang HYJ, Woods AS. Direct tissue analysis of phospholipids in rat brain using MALDI-TOFMS and MALDI-ion mobility-TOFMS. J Am Soc Mass Spectrom. 2005;16(2):133–8.
Aerni HR, Cornett DS, Caprioli RM. Automated acoustic matrix deposition for MALDI sample preparation. Anal Chem. 2006;78(3):827–34.
Claridge TDW. High-resolution NMR techniques in organic chemistry. San Diego: Elsevier; 1999.
Pochapsky TC, Pochapsky SS. NMR for physical and biological scientists. New York: Taylor & Francis; 2007.
Sanders JKM, Hunter BK. Modern NMR spectroscopy. A guide for chemists. Oxford: Oxford University Press; 1987.
Meneses P, Glonek T. P-31 NMR lipid analysis from biological sources. Biophys J. 1988;53(2):A200.
Branca M, et al. 31P nuclear magnetic resonance analysis of phospholipids in a ternary homogeneous system. Anal Biochem. 1995;232(1):1–6.
Bosco MC, Culeddu N, Toffanin R, Pollesello P. Organic solvent systems for 31P nuclear magnetic resonance analysis of lecithin phospholipids: applications to two-dimensional gradient-enhanced 1H-detected heteronuclear multiple quantum coherence experiments. Anal Biochem. 1997;245(1):38–47.
Edzes HT, et al. Analysis of phospholipids in brain tissue by 31P NMR at different compositions of the solvent system chloroform-methanol-water. Magn Reson Med. 1992;26(1):46–59.
Culeddu N, et al. 31P NMR analysis of phospholipids in crude extracts from different sources: improved efficiency of the solvent system. Magn Reson Chem. 1998;36(12):907–12.
Pearce JM, Komoroski RA. Analysis of phospholipid molecular species in brain by 31P NMR spectroscopy. Magn Reson Med. 2000;44(2):215–23.
Gorestein DG, editor. Phosphorus-31 NMR: principles and applications. San Francisco: Academic; 1984. p. 7–36.
Sotirhos N, Herslof B, Kenne L. Quantitative analysis of phospholipids by 31P-NMR. J Lipid Res. 1986;27(4):386–92.
Baumann CG, et al. Lipid differentiation in MP26 junction enriched membranes of bovine lens fiber cells. Biochim Biophys Acta. 1996;1303(2):145–53.
Estrada R, Borchman D, Yappert MC. Tracking phospholipid biogenesis by MALDI-TOFMS. Biophys J. 2005;88(1):354A.
Pearce JM, Komoroski RA. Analysis of phospholipid molecular species in brain by P-31 NMR spectroscopy. Magn Reson Med. 2000;44(2):215–23.
Estrada R, Stolowich N, Yappert MC. Influence of temperature on P-31 NMR chemical shifts of phospholipids and their metabolites. I. In chloroform-methanol-water. Anal Biochem. 2008;380(1):41–50.
Chen Y, et al. Facial amphiphiles. J Am Chem Soc. 1992;114(18):7319–20.
Hildebrand A, et al. Solubilization of negatively charged DPPC/DPPG liposomes by bile salts. J Colloid Interface Sci. 2004;279(2):559–71.
Hildebrand A, et al. Thermodynamics of demicellization of mixed micelles composed of sodium oleate and bile salts. Langmuir. 2004;20(2):320–8.
Hildebrand A, et al. Temperature dependence of the interaction of cholate and deoxycholate with fluid model membranes and their solubilization into mixed micelles. Colloid Surf B. 2003;32(4):335–51.
Hildebrand A, et al. Bile salt induced solubilization of synthetic phosphatidylcholine vesicles studied by isothermal titration calorimetry. Langmuir. 2002;18(7):2836–47.
Garidel P, et al. Thermodynamic characterization of bile salt aggregation as a function of temperature and ionic strength using isothermal titration calorimetry. Langmuir. 2000;16(12):5267–75.
Santhanalakshmi J, et al. Small-angle neutron scattering study of sodium cholate and sodium deoxycholate interacting micelles in aqueous medium. Proc Indian Acad Sci (Chem Sci). 2001;113(1):55–62.
Komoroski RA, et al. Phospholipid abnormalities in postmortem schizophrenic brains detected by P-31 nuclear magnetic resonance spectroscopy: a preliminary study. Psychiat Res Neuroim. 2001;106(3):171–80.
Pearce JM, et al. Analysis of saturated phosphatidylcholine in amniotic-fluid by P-31 NMR. Magn Reson Med. 1993;30(4):476–84.
Pearce JM, et al. Analysis of phospholipids in human amniotic fluid by 31P NMR. Magn Reson Med. 1991;21(1):107–16.
Pearce JM, Komoroski RA. Resolution of phospholipid molecular species by 31P NMR. Magn Reson Med. 1993;29(6):724–31.
Schiller J, Arnold K. Application of high resolution 31P NMR spectroscopy to the characterization of the phospholipid composition of tissues and body fluids—a methodological review. Med Sci Monit. 2002;8(11):205–22.
Puppato A, et al. Effect of temperature and pH on P-31 nuclear magnetic resonances of phospholipids in cholate micelles. Chem Phys Lipids. 2007;150(2):176–85.
Estrada R, et al. Re-evaluation of the phospholipids composition in membranes of adult human lenses. Biochim Biophys Acta- Biomembranes. 2010;1798(3):303–311.
Acknowledgments
The ongoing, 25-year collaboration with Professor Douglass Borchman is most deeply appreciated. The discussions and generous donation of animal ocular tissue by the former Director of the Louisville Zoo, Dr. William Foster, and current veterinarians, Dr. Roy Burns and Dr. Zoole Gymesi are thankfully acknowledged. Professor Donald DuPré’s theoretical predictions of P-31 chemical shifts have been most helpful for the interpretation of experimental trends. Without the funding provided by the National Eye Institute many of the studies cited in this chapter would not have been completed. Finally, to the many students in our graduate program that carried out these studies, a heartfelt thank-you.
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Glossary
- AAN
-
2-(2-Aminoethylamino)-5-nitropyridine; a basic organic matrix that promotes the generation of anions.
- APCI
-
Atmospheric pressure chemical ionization.
- DHB
-
2,5-Dihydroxybenzoic acid, one of the matrices most commonly used for the MALDI-MS analysis of small molecules, including phospholipids. Its acidic character facilitates the formation of cations.
- Electrospray/nanospray
-
Mild ionization technique involving nebularization and a high electric field at a metallic nozzle. Compatible with online chromatography as well as direct infusion, and results primarily in molecular ions.
- MALDI
-
Matrix-assisted laser desorption/ionization, a commonly used means of ionizing and vaporizing an analyte for introduction into a mass spectrometer.
- PC, PE, PI, PS
-
Phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine, common phospholipids (PL) differing at the head group moiety.
- Plasmalogens
-
Ether lipids where the first position of glycerol bears a vinyl residue in an ether linkage rather than an ester. The double bond next to the ether bond.
- PNA
-
Para-nitroaniline, a nearly neutral matrix used in the MALDI-MS analysis of phospholipids in both positive and negative modes. It also enables imaging of phospholipids in tissues.
- Sphingolipids
-
Class of lipids based on sphingosine, which has a serine backbone. Different derivatives on the serine hydroxyl give different family members such as ceramide and sphingomyelin (SM).
- Temperature coefficient
-
Variation of, for example, chemical shift with temperature. Often linear, and then defined as dδ/dT. The sign and magnitude may provide clues about interactions, such as hydrogen bonding.
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Yappert, M.C. (2012). Compositional Analysis of Phospholipids by Mass Spectrometry and Phosphorus-31 Nuclear Magnetic Resonance Spectroscopy. In: Fan, TM., Lane, A., Higashi, R. (eds) The Handbook of Metabolomics. Methods in Pharmacology and Toxicology. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-618-0_12
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