메뉴 건너뛰기




Volumn 75, Issue 6, 1998, Pages 2932-2946

The mechanism of detergent solubilization of liposomes and protein- containing membranes

Author keywords

[No Author keywords available]

Indexed keywords

DETERGENT; DODECYL SULFATE SODIUM; LIPOSOME; PROTEIN;

EID: 0031770290     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77735-5     Document Type: Article
Times cited : (277)

References (64)
  • 2
    • 70449246528 scopus 로고
    • Phosphorous assay in column chromatography
    • Bartlett, G. R. 1959. Phosphorous assay in column chromatography. J. Biol. Chem. 234:466-468.
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 3
    • 0023666940 scopus 로고
    • Phospholipid fatty acyl chain asymmetry in the membrane bilayer of isolated skeletal muscle sarcoplasmic reticulum
    • Bick, R. J., W. B. Van Winkle, C. A. Tate, and M. L. Entman. 1987. Phospholipid fatty acyl chain asymmetry in the membrane bilayer of isolated skeletal muscle sarcoplasmic reticulum. Biochemistry. 26: 4831-4836.
    • (1987) Biochemistry , vol.26 , pp. 4831-4836
    • Bick, R.J.1    Van Winkle, W.B.2    Tate, C.A.3    Entman, M.L.4
  • 5
    • 0343948794 scopus 로고
    • Liposomes in reconstitution of ion-pumps
    • Y. Barenholz and D. D. Lasic, editors. CRC Press, Boca Raton,. FL
    • Cornelius, F., and J. V. Møller. 1995. Liposomes in reconstitution of ion-pumps. In Handbook of Nonmedical Applications of Liposomes. Vol. II. Y. Barenholz and D. D. Lasic, editors. CRC Press, Boca Raton,. FL. 219-243.
    • (1995) Handbook of Nonmedical Applications of Liposomes , vol.2 , pp. 219-243
    • Cornelius, F.1    Møller, J.V.2
  • 7
    • 0029030012 scopus 로고
    • 2-D structure of the Neurospora crassa plasma membrane ATPase as determined by electron cryomicroscopy
    • Cyrklaff, M., M. Auer, W. Kühlbrandt, and G. A. Scarborough. 1995. 2-D structure of the Neurospora crassa plasma membrane ATPase as determined by electron cryomicroscopy. EMBO J. 14:1854-1857.
    • (1995) EMBO J. , vol.14 , pp. 1854-1857
    • Cyrklaff, M.1    Auer, M.2    Kühlbrandt, W.3    Scarborough, G.A.4
  • 12
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution
    • Deisenhofer, J., O. Epp, K. Miki, R. Huber, and H. Michel. 1985. Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution. Nature. 318:618-621.
    • (1985) Nature , vol.318 , pp. 618-621
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 15
    • 0002183955 scopus 로고
    • Effects of Triton X-100 on sonicated lecithin vesicles
    • Edwards, K., M. Almgren, J. Bellare, and W. Brown. 1989. Effects of Triton X-100 on sonicated lecithin vesicles. Langmuir. 5:473-478.
    • (1989) Langmuir , vol.5 , pp. 473-478
    • Edwards, K.1    Almgren, M.2    Bellare, J.3    Brown, W.4
  • 16
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipides from animal tissues
    • Folch, J., M. Lee, and G. H. S. Stanley. 1957. A simple method for the isolation and purification of total lipides from animal tissues. J. Biol. Chem. 266:497-509.
    • (1957) J. Biol. Chem. , vol.266 , pp. 497-509
    • Folch, J.1    Lee, M.2    Stanley, G.H.S.3
  • 17
    • 37049076711 scopus 로고
    • From discoid micelles to spherical vesicles: The concept of edge activity
    • Fromherz, P., C. Röcker, and D. Rüppel. 1986. From discoid micelles to spherical vesicles: the concept of edge activity. Faraday Discuss. Chem. Soc. 81:39-48.
    • (1986) Faraday Discuss. Chem. Soc. , vol.81 , pp. 39-48
    • Fromherz, P.1    Röcker, C.2    Rüppel, D.3
  • 20
    • 0028598233 scopus 로고
    • Membrane water partitioning of oligo(ethylene oxide) dodecyl ethers and its relevance for solubilization
    • Heerklotz, H., H. Binder, G. Lantzsch, G., and G. Klose. 1994. Membrane water partitioning of oligo(ethylene oxide) dodecyl ethers and its relevance for solubilization. Biochim. Biophys. Acta. 1196:114-122.
    • (1994) Biochim. Biophys. Acta , vol.1196 , pp. 114-122
    • Heerklotz, H.1    Binder, H.2    Lantzsch, G.G.3    Klose, G.4
  • 22
    • 0028890031 scopus 로고
    • Structure at 2. Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., C. Ostermeier, B. Ludwig, and H. Michel. 1995. Structure at 2. Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 24
    • 0001684352 scopus 로고
    • Surfactant interactions with biomembranes and proteins
    • Jones, M. N. 1992. Surfactant interactions with biomembranes and proteins. Chem. Res. 21:127-136
    • (1992) Chem. Res. , vol.21 , pp. 127-136
    • Jones, M.N.1
  • 25
    • 0023772728 scopus 로고
    • +-ATPase: Enzyme sources, preparative problems and preparation from mammalian kidney
    • +-ATPase: enzyme sources, preparative problems and preparation from mammalian kidney. Methods Enzymol. 156:29-43.
    • (1988) Methods Enzymol. , vol.156 , pp. 29-43
    • 1    Rgensen, P.L.2
  • 26
    • 33847085064 scopus 로고
    • Characterization of micellar solutions using surfactant electrodes
    • Kale, K. C., E. L. Cussler, and D. F. Evans. 1980. Characterization of micellar solutions using surfactant electrodes. J. Phys. Chem. 84: 593-598.
    • (1980) J. Phys. Chem. , vol.84 , pp. 593-598
    • Kale, K.C.1    Cussler, E.L.2    Evans, D.F.3
  • 27
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann, W. 1959. Some factors in the interpretation of protein denaturation. Adv. Protein Chem. 14:1-63.
    • (1959) Adv. Protein Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 28
    • 0027477920 scopus 로고
    • Transitional steps in the solubilization ot protein-containing membranes and liposomes by non-ionic detergent
    • Kragh-Hansen, U., M. le Maire, J.-P. Noël, T. Gulik-Krzywick, and J. V. Møller. 1993. Transitional steps in the solubilization ot protein-containing membranes and liposomes by non-ionic detergent. Biochemistry. 32:1648-1656.
    • (1993) Biochemistry , vol.32 , pp. 1648-1656
    • Kragh-Hansen, U.1    Le Maire, M.2    Noël, J.-P.3    Gulik-Krzywick, T.4    Møller, J.V.5
  • 30
    • 0029088548 scopus 로고
    • Interaction of detergents with lipid vesicles
    • Lasch, J. 1995. Interaction of detergents with lipid vesicles. Biochim. Biophys. Acta. 1241:269-292.
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 269-292
    • Lasch, J.1
  • 31
    • 0020489065 scopus 로고
    • A molecular model of vesicle formation
    • Lasic, D. D. 1982. A molecular model of vesicle formation. Biochim. Biophys. Acta. 692:501-505.
    • (1982) Biochim. Biophys. Acta , vol.692 , pp. 501-505
    • Lasic, D.D.1
  • 32
    • 0024289274 scopus 로고
    • The mechanism of vesicle formation
    • Lasic, D. D. 1988. The mechanism of vesicle formation. Biochem. J. 256:1-11.
    • (1988) Biochem. J. , vol.256 , pp. 1-11
    • Lasic, D.D.1
  • 34
    • 0020657411 scopus 로고
    • Mode of interaction of polyethylene glycol detergents with membrane proteins
    • le Maire M., S. Kwee, J. P. Andersen, and J. V. Møller. 1983. Mode of interaction of polyethylene glycol detergents with membrane proteins. Eur. J. Biochem. 129:525-535.
    • (1983) Eur. J. Biochem. , vol.129 , pp. 525-535
    • Le Maire, M.1    Kwee, S.2    Andersen, J.P.3    Møller, J.V.4
  • 35
    • 0023666958 scopus 로고
    • Binding of a nonionic detergent to membranes: Flip-flop rate and location on the bilayer
    • le Maire, M., J. V. Møller, and P. Champeil. 1987. Binding of a nonionic detergent to membranes: flip-flop rate and location on the bilayer. Biochemistry. 26:4803-4810.
    • (1987) Biochemistry , vol.26 , pp. 4803-4810
    • Le Maire, M.1    Møller, J.V.2    Champeil, P.3
  • 36
    • 0025077724 scopus 로고
    • Phospholipid vesicle solubilization and reconstitution by detergents. Symmetrical analysis of the two processes using octaethylene glycol mono-n-dodecyl ether
    • Levy, D., A. Gulik, M. Seigneuret, and J.-L. Rigaud. 1990. Phospholipid vesicle solubilization and reconstitution by detergents. Symmetrical analysis of the two processes using octaethylene glycol mono-n-dodecyl ether. Biochemistry. 29:9480-9488.
    • (1990) Biochemistry , vol.29 , pp. 9480-9488
    • Levy, D.1    Gulik, A.2    Seigneuret, M.3    Rigaud, J.-L.4
  • 37
    • 0022348630 scopus 로고
    • Characterization of the solubilization of lipid bilayers by surfactants
    • Lichtenberg, D. 1985. Characterization of the solubilization of lipid bilayers by surfactants. Biochim. Biophys. Acta. 821:470-478.
    • (1985) Biochim. Biophys. Acta , vol.821 , pp. 470-478
    • Lichtenberg, D.1
  • 38
    • 0000339108 scopus 로고
    • Liposomes as a model for solubilization and reconstitution of membranes
    • Y. Barenholz and D. D. Lasic, editors. CRC Press, Boca Raton, FL
    • Lichtenberg, D. 1995. Liposomes as a model for solubilization and reconstitution of membranes. In Handbook of Nonmedical Applications of Liposomes, Vol. II. Y. Barenholz and D. D. Lasic, editors. CRC Press, Boca Raton, FL. 199-218.
    • (1995) Handbook of Nonmedical Applications of Liposomes , vol.2 , pp. 199-218
    • Lichtenberg, D.1
  • 39
    • 0021111031 scopus 로고
    • Solubilization of phospholipid by detergents. Structural and kinetic aspects
    • Lichtenberg, D., R. J. Robson, and E. A. Dennis. 1983. Solubilization of phospholipid by detergents. Structural and kinetic aspects. Biochim. Biophys. Acta. 737:285-304.
    • (1983) Biochim. Biophys. Acta , vol.737 , pp. 285-304
    • Lichtenberg, D.1    Robson, R.J.2    Dennis, E.A.3
  • 40
    • 0032562793 scopus 로고    scopus 로고
    • Direct formation of mixed micelles in the solubilization of phospholipid liposomes by Triton X-100
    • López, O., A. De la Maza, L. Coderch, C. López-Iglesias, E. Wehrli, and J. L. Parra. 1998. Direct formation of mixed micelles in the solubilization of phospholipid liposomes by Triton X-100. FEBS Lett. 426: 314-318.
    • (1998) FEBS Lett. , vol.426 , pp. 314-318
    • López, O.1    De La Maza, A.2    Coderch, L.3    López-Iglesias, C.4    Wehrli, E.5    Parra, J.L.6
  • 42
    • 0016361465 scopus 로고
    • Isolation of proteins of sarcoplasmic reticulum
    • MacLennan, D. H. 1974. Isolation of proteins of sarcoplasmic reticulum. Methods Enzymol. 32:291-302.
    • (1974) Methods Enzymol. , vol.32 , pp. 291-302
    • MacLennan, D.H.1
  • 43
    • 0002182090 scopus 로고
    • Physical characterization of liposomes for understanding structure-function relationships in biological membranes
    • Y. Barenholz and D. D. Lasic, editors. CRC Press, Boca Raton, FL
    • Marsh, D. 1995. Physical characterization of liposomes for understanding structure-function relationships in biological membranes. In Handbook of Nonmedical Applications of Liposomes, Vol II. Y. Barenholz and D. D. Lasic, editors. CRC Press, Boca Raton, FL. 1-20.
    • (1995) Handbook of Nonmedical Applications of Liposomes , vol.2 , pp. 1-20
    • Marsh, D.1
  • 44
  • 46
    • 0027283560 scopus 로고
    • Detergent binding as a measure of hydrophobic surface area of integral membrane proteins
    • Møller, J. V., and M. le Maire. 1993. Detergent binding as a measure of hydrophobic surface area of integral membrane proteins. J. Biol. Chem. 268:18659-18672.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18659-18672
    • Møller, J.V.1    Le Maire, M.2
  • 47
    • 0000559797 scopus 로고
    • Uses of non-ionic and bile salt detergents in the study of membrane proteins
    • A. Watts and J. J. H. H. M. de Pont, editors. Elsevier Biochemical Press, Amsterdam
    • Møller, J. V., M. le Maire, and J. P. Andersen. 1986. Uses of non-ionic and bile salt detergents in the study of membrane proteins. In Progress in Protein-Lipid Interactions, Vol 2. A. Watts and J. J. H. H. M. de Pont, editors. Elsevier Biochemical Press, Amsterdam. 147-196.
    • (1986) Progress in Protein-Lipid Interactions , vol.2 , pp. 147-196
    • Møller, J.V.1    Le Maire, M.2    Andersen, J.P.3
  • 48
    • 0003747158 scopus 로고
    • Dilute solutions of amphipathic ions. I. Conductivity of strong salts and dimerization
    • Mukerjee, P., K. J. Mysels, and C. I. Dulin. 1958. Dilute solutions of amphipathic ions. I. Conductivity of strong salts and dimerization. J. Phys. Chem. 62:1390-1396.
    • (1958) J. Phys. Chem. , vol.62 , pp. 1390-1396
    • Mukerjee, P.1    Mysels, K.J.2    Dulin, C.I.3
  • 49
    • 0030732619 scopus 로고    scopus 로고
    • Exchange of monooleoyl phosphatidylcholine as monomer and micelle with membranes containing poly(ethylene glycol)-lipid
    • Needham, D., N. Stoicheva, and D. V. Zhelev. 1997. Exchange of monooleoyl phosphatidylcholine as monomer and micelle with membranes containing poly(ethylene glycol)-lipid. Biophys. J. 73:2615-2629.
    • (1997) Biophys. J. , vol.73 , pp. 2615-2629
    • Needham, D.1    Stoicheva, N.2    Zhelev, D.V.3
  • 50
    • 0024281314 scopus 로고
    • Micelle vesicle transition of egg phosphatidylcholine and octyl glucoside
    • Ollivon, M., O. Eidelman, R. Blumenthal, and A. Walter. 1988. Micelle vesicle transition of egg phosphatidylcholine and octyl glucoside. Biochemistry. 27:1695-1703.
    • (1988) Biochemistry , vol.27 , pp. 1695-1703
    • Ollivon, M.1    Eidelman, O.2    Blumenthal, R.3    Walter, A.4
  • 51
    • 0028797071 scopus 로고
    • 8 as studied by deuterium- and phosphorous-NMR, light scattering, and calorimetry
    • 8 as studied by deuterium- and phosphorous-NMR, light scattering, and calorimetry. Biophys. J. 68:584-597.
    • (1995) Biophys. J. , vol.68 , pp. 584-597
    • Otten, D.1    Löbbecke, L.2    Beyer, K.3
  • 52
    • 0028857088 scopus 로고
    • Partition coefficient of a surfactant between aggregates and solution: Application to micelle-vesicle transition of egg phosphatidylcholine and octyl-β-D-glucoside
    • Paternostre, M. T., O. Meyer, C. Grabielle-Madelmont, S. Lesieur, M. Ghanam, and M. Ollivon. 1995. Partition coefficient of a surfactant between aggregates and solution: application to micelle-vesicle transition of egg phosphatidylcholine and octyl-β-D-glucoside. Biophys. J. 69:2476-2488.
    • (1995) Biophys. J. , vol.69 , pp. 2476-2488
    • Paternostre, M.T.1    Meyer, O.2    Grabielle-Madelmont, C.3    Lesieur, S.4    Ghanam, M.5    Ollivon, M.6
  • 53
    • 0024291653 scopus 로고
    • Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving detergents. 1. Solubilization of large unilamellar liposomes (prepared by reverse-phase evaporation) by Triton X-100, octyl glucoside and sodium cholate
    • Paternostre, M. T., M. Roux, and J.-L. Rigaud. 1988. Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving detergents. 1. Solubilization of large unilamellar liposomes (prepared by reverse-phase evaporation) by Triton X-100, octyl glucoside and sodium cholate. Biochemistry. 27:2668-2676.
    • (1988) Biochemistry , vol.27 , pp. 2668-2676
    • Paternostre, M.T.1    Roux, M.2    Rigaud, J.-L.3
  • 54
    • 0023583873 scopus 로고
    • Refolding of bacteriorhodopsin in lipid bilayers. a thermodynamically controlled two-stage process
    • Popot, J.-L., S.-E. Gerchmain, and D. M. Engelman. 1987. Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process. J. Mol. Biol. 198:655-676.
    • (1987) J. Mol. Biol. , vol.198 , pp. 655-676
    • Popot, J.-L.1    Gerchmain, S.-E.2    Engelman, D.M.3
  • 55
    • 0014063229 scopus 로고
    • The binding of divers detergent anions to bovine serum albumin
    • Reynolds, J. A., S. Herbert, H. Polet, and J. Steinhardt. 1967. The binding of divers detergent anions to bovine serum albumin. Biochemistry. 6:937-947.
    • (1967) Biochemistry , vol.6 , pp. 937-947
    • Reynolds, J.A.1    Herbert, S.2    Polet, H.3    Steinhardt, J.4
  • 56
    • 0021760481 scopus 로고
    • 31P NMR as a tool for monitoring detergent solubilization of sarcoplasmic reticulum membranes
    • 31P NMR as a tool for monitoring detergent solubilization of sarcoplasmic reticulum membranes. FEBS Lett. 171:169-172.
    • (1984) FEBS Lett. , vol.171 , pp. 169-172
    • Roux, M.1    Champeil, P.2
  • 57
    • 0029941453 scopus 로고    scopus 로고
    • Vesicle solubilization by alkyl sulfate surfactants: A cryo-TEM study of the vesicle to micelle transition
    • Silvander, M., G. Karlsson, and K. Edwards. 1996. Vesicle solubilization by alkyl sulfate surfactants: a cryo-TEM study of the vesicle to micelle transition. J. Colloid Interface Sci. 179:104-113.
    • (1996) J. Colloid Interface Sci. , vol.179 , pp. 104-113
    • Silvander, M.1    Karlsson, G.2    Edwards, K.3
  • 59
    • 0015505878 scopus 로고
    • Hydrophobic free energy, micelle formation and the association of proteins with amphiphiles
    • Tanford, C. 1972. Hydrophobic free energy, micelle formation and the association of proteins with amphiphiles. J. Mol. Biol. 67:59-71.
    • (1972) J. Mol. Biol. , vol.67 , pp. 59-71
    • Tanford, C.1
  • 61
    • 0027512587 scopus 로고
    • Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane
    • Toyoshima, C., H. Sasabe, and D. L. Stokes. 1993. Three-dimensional cryo-electron microscopy of the calcium ion pump in the sarcoplasmic reticulum membrane. Nature. 362:467-471.
    • (1993) Nature , vol.362 , pp. 467-471
    • Toyoshima, C.1    Sasabe, H.2    Stokes, D.L.3
  • 62
    • 0024745128 scopus 로고
    • Vesicle-micelle transition of phosphatidylcholine and octylglucoside elucidated by cryotransmission electron microscopy
    • Vinson, P. K., Y. Talmon, and A. Walter. 1989. Vesicle-micelle transition of phosphatidylcholine and octylglucoside elucidated by cryotransmission electron microscopy. Biophys. J. 56:669-681.
    • (1989) Biophys. J. , vol.56 , pp. 669-681
    • Vinson, P.K.1    Talmon, Y.2    Walter, A.3
  • 64
    • 0030893617 scopus 로고    scopus 로고
    • Octyl-β-D-glucopyranoside partitioning into lipid bilayers. Thermodynamics of binding and structural changes of the bilayer
    • Wenk, M. R., T. Alt, A. Seelig, and J. Seelig. 1997. Octyl-β-D-glucopyranoside partitioning into lipid bilayers. Thermodynamics of binding and structural changes of the bilayer. Biophys. J. 72:1719-1731.
    • (1997) Biophys. J. , vol.72 , pp. 1719-1731
    • Wenk, M.R.1    Alt, T.2    Seelig, A.3    Seelig, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.