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Volumn 83, Issue 5, 2001, Pages 387-397

Novel methods for studying lipids and lipases and their mutual interaction at interfaces. Part I. Atomic force microscopy

Author keywords

Atomic force microscopy; Lipase; Lipase hydrolysis and kinetics

Indexed keywords

LIPID; PHOSPHOLIPASE A2; TRIACYLGLYCEROL LIPASE;

EID: 0035021048     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(01)01264-0     Document Type: Review
Times cited : (59)

References (90)
  • 3
    • 0000641604 scopus 로고    scopus 로고
    • Supramolecular organization of highly conducting organic thin films by the Langmuir-Blodgett technique
    • Bjørnholm T., Hassenkam T., Reitzel N. Supramolecular organization of highly conducting organic thin films by the Langmuir-Blodgett technique. J. Mat. Chem. 9:1999;1975-1990.
    • (1999) J. Mat. Chem. , vol.9 , pp. 1975-1990
    • Bjørnholm, T.1    Hassenkam, T.2    Reitzel, N.3
  • 4
    • 0032479388 scopus 로고    scopus 로고
    • Lipases: Interfacial enzymes with attractive applications
    • Schmid R.D., Verger R. Lipases: Interfacial enzymes with attractive applications. Angew. Chem. Int. 37:1998;1608-1633.
    • (1998) Angew. Chem. Int , vol.37 , pp. 1608-1633
    • Schmid, R.D.1    Verger, R.2
  • 5
    • 0001248967 scopus 로고    scopus 로고
    • The role of enzymes in modern detergency
    • Olsen H.S., Falholt P. The role of enzymes in modern detergency. J. Surfact. Deterg. 1:1998;555-567.
    • (1998) J. Surfact. Deterg. , vol.1 , pp. 555-567
    • Olsen, H.S.1    Falholt, P.2
  • 6
    • 0342466038 scopus 로고    scopus 로고
    • J.H. van Ee, O. Misset, Baas E.J. New York: Marcel Dekker Inc
    • van Ee J.H, Misset O, Baas E.J. Enzymes in detergency, Surfactant Sciences. Vol. 69:1997;Marcel Dekker Inc, New York.
    • (1997) Enzymes in Detergency, Surfactant Sciences , vol.69
  • 8
    • 5244305946 scopus 로고
    • The constitution and fundamental properties of solids and liquids. II. Liquids
    • Langmuir I. The constitution and fundamental properties of solids and liquids. II. Liquids. J. Am. Chem. Soc. 39:1917;1848-1906.
    • (1917) J. Am. Chem. Soc. , vol.39 , pp. 1848-1906
    • Langmuir, I.1
  • 11
    • 0032911920 scopus 로고    scopus 로고
    • Bacterial S-layer protein coupling to lipids: X-ray reflectivity and grazing incidence diffraction studies
    • Weygand W., Wetzer B., Pum D., Sleytr U.B., Cuvillier N., Kjaer K., Howes P., Lösche M. Bacterial S-layer protein coupling to lipids: X-ray reflectivity and grazing incidence diffraction studies. Biophys. J. 76:1999;458-468.
    • (1999) Biophys. J. , vol.76 , pp. 458-468
    • Weygand, W.1    Wetzer, B.2    Pum, D.3    Sleytr, U.B.4    Cuvillier, N.5    Kjaer, K.6    Howes, P.7    Lösche, M.8
  • 13
    • 33947349896 scopus 로고
    • Monomolecular films of fatty acids on glass
    • Blodgett K.B. Monomolecular films of fatty acids on glass. J. Am. Chem. Soc. 56:1934;495-495.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 495-495
    • Blodgett, K.B.1
  • 14
    • 33847456945 scopus 로고
    • Films built by depositing successive monomolecular layers on a solid surface
    • Blodgett K.B. Films built by depositing successive monomolecular layers on a solid surface. J. Am. Chem. Soc. 57:1935;1007-1022.
    • (1935) J. Am. Chem. Soc. , vol.57 , pp. 1007-1022
    • Blodgett, K.B.1
  • 21
    • 0030061086 scopus 로고    scopus 로고
    • Comparative atomic force and scanning electron microscopy: An investigation on fenestrated endothelial cells in vitro
    • Braet F., Kalle W.H., De Zanger R.B., De Grooth B.G., Raap A.K., Tanke H.J., Wisse E. Comparative atomic force and scanning electron microscopy: an investigation on fenestrated endothelial cells in vitro. J. Microsc. 181:1996;10-17.
    • (1996) J. Microsc. , vol.181 , pp. 10-17
    • Braet, F.1    Kalle, W.H.2    De Zanger, R.B.3    De Grooth, B.G.4    Raap, A.K.5    Tanke, H.J.6    Wisse, E.7
  • 22
    • 0031860049 scopus 로고    scopus 로고
    • Imaging surface and submembraneous structures with the atomic force microscope: A study on living cancer cells, fibroblasts and macrophages
    • Braet F., Seynaeve C., De Zanger R., Wisse E. Imaging surface and submembraneous structures with the atomic force microscope: a study on living cancer cells, fibroblasts and macrophages. J. Microsc. 190:1998;328-338.
    • (1998) J. Microsc. , vol.190 , pp. 328-338
    • Braet, F.1    Seynaeve, C.2    De Zanger, R.3    Wisse, E.4
  • 24
    • 0028215348 scopus 로고
    • Granula motion and membrane spreading during activation of human platelets imaged by atomic force microscopy
    • Fritz M., Radmacher M., Gaub H. Granula motion and membrane spreading during activation of human platelets imaged by atomic force microscopy. Biophys J. 66:1994;1328-1334.
    • (1994) Biophys J. , vol.66 , pp. 1328-1334
    • Fritz, M.1    Radmacher, M.2    Gaub, H.3
  • 25
    • 0027167430 scopus 로고
    • Cytoskeleton of living, unstained cells imaged by scanning force microscopy
    • Chang L., Kious T., Yorgancioglu M., Keller D., Pfeifer J. Cytoskeleton of living, unstained cells imaged by scanning force microscopy. Biophys. J. 64:1993;1282-1286.
    • (1993) Biophys. J. , vol.64 , pp. 1282-1286
    • Chang, L.1    Kious, T.2    Yorgancioglu, M.3    Keller, D.4    Pfeifer, J.5
  • 26
    • 0032042161 scopus 로고    scopus 로고
    • Optimization and utilization of the atomic force microscope for living systems
    • Dvorak J.A., Nagao E. Optimization and utilization of the atomic force microscope for living systems. Scanning. 20:1998;138-139.
    • (1998) Scanning , vol.20 , pp. 138-139
    • Dvorak, J.A.1    Nagao, E.2
  • 27
    • 0028215348 scopus 로고
    • Granula motion and membrane spreading during activation of human platelets imaged by atomic force microscopy
    • Fritz M., Radmacher M., Gaub H. Granula motion and membrane spreading during activation of human platelets imaged by atomic force microscopy. Biophys J. 66:1994;1328-1334.
    • (1994) Biophys J. , vol.66 , pp. 1328-1334
    • Fritz, M.1    Radmacher, M.2    Gaub, H.3
  • 30
    • 0033105817 scopus 로고    scopus 로고
    • Salt-dependent chromosome viscoelasticity characterized by scanning force microscopy-based volume measurements
    • Fritzsche W. Salt-dependent chromosome viscoelasticity characterized by scanning force microscopy-based volume measurements. Microsc. Res. Tech. 44:1999;357-362.
    • (1999) Microsc. Res. Tech. , vol.44 , pp. 357-362
    • Fritzsche, W.1
  • 31
    • 0029791094 scopus 로고    scopus 로고
    • Scanning force microscopy reveals ellipsoid shape of chicken erythrocyte nucleosomes
    • Fritzsche W., Henderson E. Scanning force microscopy reveals ellipsoid shape of chicken erythrocyte nucleosomes. Biophys. J. 71:1996;2222-2226.
    • (1996) Biophys. J. , vol.71 , pp. 2222-2226
    • Fritzsche, W.1    Henderson, E.2
  • 34
    • 0025663353 scopus 로고
    • Imaging the membrane protein bacteriorhodopsin with the atomic force microscope
    • Butt H.J., Downing K.H., Hansma P.K. Imaging the membrane protein bacteriorhodopsin with the atomic force microscope. Biophys. J. 58:1990;1473-1480.
    • (1990) Biophys. J. , vol.58 , pp. 1473-1480
    • Butt, H.J.1    Downing, K.H.2    Hansma, P.K.3
  • 36
    • 0026095474 scopus 로고
    • Atomic force microscopy and dissection of gap junctions
    • Hoh J.H., Lal R., John S.A., Revel J.P., Arnsdorf M.F. Atomic force microscopy and dissection of gap junctions. Science. 253:1991;1405-1408.
    • (1991) Science , vol.253 , pp. 1405-1408
    • Hoh, J.H.1    Lal, R.2    John, S.A.3    Revel, J.P.4    Arnsdorf, M.F.5
  • 37
    • 0029989164 scopus 로고    scopus 로고
    • Directly probing rapid membrane protein dynamics with an atomic force microscope: A study of light-induced conformational alterations in bacteriorhodopsin
    • Lewis A., Rousso I., Khachatryan E., Brodsky I., Lieberman K., Sheves M. Directly probing rapid membrane protein dynamics with an atomic force microscope: a study of light-induced conformational alterations in bacteriorhodopsin. Biophys. J. 70:1996;2380-2384.
    • (1996) Biophys. J. , vol.70 , pp. 2380-2384
    • Lewis, A.1    Rousso, I.2    Khachatryan, E.3    Brodsky, I.4    Lieberman, K.5    Sheves, M.6
  • 38
    • 0037666544 scopus 로고    scopus 로고
    • Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy
    • Müller D.J., Engel A. Voltage and pH-induced channel closure of porin OmpF visualized by atomic force microscopy. J. Mol. Biol. 285:1998;1347-1351.
    • (1998) J. Mol. Biol. , vol.285 , pp. 1347-1351
    • Müller, D.J.1    Engel, A.2
  • 39
    • 0040298977 scopus 로고    scopus 로고
    • Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane
    • Müller D.J., Sass H.J., Müller S.A., Büldt G., Engel A. Surface structures of native bacteriorhodopsin depend on the molecular packing arrangement in the membrane. J. Mol. Biol. 285:1999;1903-1909.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1903-1909
    • Müller, D.J.1    Sass, H.J.2    Müller, S.A.3    Büldt, G.4    Engel, A.5
  • 40
    • 0028957621 scopus 로고
    • Imaging purple membranes in aqueous solutions at sub-nanometer resolution by atomic force microscopy
    • Müller D.J., Schabert F.A., Büldt G., Engel A. Imaging purple membranes in aqueous solutions at sub-nanometer resolution by atomic force microscopy. Biophys. J. 68:1995;1681-1686.
    • (1995) Biophys. J. , vol.68 , pp. 1681-1686
    • Müller, D.J.1    Schabert, F.A.2    Büldt, G.3    Engel, A.4
  • 41
    • 0031031403 scopus 로고    scopus 로고
    • Surface dynamics in living acinar cells images by atomic force microscopy: Identification of plasma membranes structures involved in exocytosis
    • Schneider S.W., Sritharan K.C., Geibel J.P., Oberleithner H., Jena B.P. Surface dynamics in living acinar cells images by atomic force microscopy: identification of plasma membranes structures involved in exocytosis. Proc. Natl. Acad. Sci. USA. 94:1997;316-321.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 316-321
    • Schneider, S.W.1    Sritharan, K.C.2    Geibel, J.P.3    Oberleithner, H.4    Jena, B.P.5
  • 42
    • 0008604834 scopus 로고
    • Progress in DNA-imaging: Double stranded multimers and bases of DNA deposited on the basal plane of graphite
    • Allen M., Balhorn R., Balooch M., Siekhaus W.J., Tench R.J., Subbiah S. Progress in DNA-imaging: double stranded multimers and bases of DNA deposited on the basal plane of graphite. AIP Conf. Proc. 241:1991;176-189.
    • (1991) AIP Conf. Proc. , vol.241 , pp. 176-189
    • Allen, M.1    Balhorn, R.2    Balooch, M.3    Siekhaus, W.J.4    Tench, R.J.5    Subbiah, S.6
  • 44
    • 0029252016 scopus 로고
    • Adsorption of DNA to mica, silylated mica and minerals: Characterization by atomic force microscopy
    • Bezanilla M., Manne S., Laney D.E., Lyubchenko Y.L., Hansma H.G. Adsorption of DNA to mica, silylated mica and minerals: characterization by atomic force microscopy. Langmuir. 11:1995;655-659.
    • (1995) Langmuir , vol.11 , pp. 655-659
    • Bezanilla, M.1    Manne, S.2    Laney, D.E.3    Lyubchenko, Y.L.4    Hansma, H.G.5
  • 45
    • 0029863919 scopus 로고    scopus 로고
    • DNA binding to mica correlates with cationic radius: Assay by atomic force microscopy
    • Hansma H.G., Laney D.E. DNA binding to mica correlates with cationic radius: assay by atomic force microscopy. Biophys. J. 70:1996;1933-1939.
    • (1996) Biophys. J. , vol.70 , pp. 1933-1939
    • Hansma, H.G.1    Laney, D.E.2
  • 47
    • 0033052687 scopus 로고    scopus 로고
    • Atomic force microscopy imaging of DNA covalently immobilized on a functionalized mica substrate
    • Shlyakhtenko L.S., Gall A.A., Wiemer J.J., Hawn D.D., Lyubchenko Y.L. Atomic force microscopy imaging of DNA covalently immobilized on a functionalized mica substrate. Biophys. J. 77:1999;568-576.
    • (1999) Biophys. J. , vol.77 , pp. 568-576
    • Shlyakhtenko, L.S.1    Gall, A.A.2    Wiemer, J.J.3    Hawn, D.D.4    Lyubchenko, Y.L.5
  • 49
    • 0029935874 scopus 로고    scopus 로고
    • The interaction of DNA with bacteriophage phi 29 connector: A study by AFM and TEM
    • Valle M., Valpuesta J.M., Carrascosa J.L., Tamayo J., Garcia R. The interaction of DNA with bacteriophage phi 29 connector: a study by AFM and TEM. J. Struct. Biol. 116:1996;390-398.
    • (1996) J. Struct. Biol. , vol.116 , pp. 390-398
    • Valle, M.1    Valpuesta, J.M.2    Carrascosa, J.L.3    Tamayo, J.4    Garcia, R.5
  • 51
    • 0033591349 scopus 로고    scopus 로고
    • High-resolution AFM-imaging and mechanistic analysis of the 20 S proteasome
    • Dorn I.T., Eschrich R., Seemuller E., Guckenberger R., Tampe R. High-resolution AFM-imaging and mechanistic analysis of the 20 S proteasome. J. Mol. Biol. 288:1999;1027-1036.
    • (1999) J. Mol. Biol. , vol.288 , pp. 1027-1036
    • Dorn, I.T.1    Eschrich, R.2    Seemuller, E.3    Guckenberger, R.4    Tampe, R.5
  • 52
    • 0025647578 scopus 로고
    • Direct visualization of phosphorylase-phosphorylase kinase complexes by scanning tunneling and atomic force microscopy
    • Edstrom R.D., Meinke M.H., Yang X.R., Yang R., Elings V., Evans D.F. Direct visualization of phosphorylase-phosphorylase kinase complexes by scanning tunneling and atomic force microscopy. Biophys. J. 58:1990;1437-1448.
    • (1990) Biophys. J. , vol.58 , pp. 1437-1448
    • Edstrom, R.D.1    Meinke, M.H.2    Yang, X.R.3    Yang, R.4    Elings, V.5    Evans, D.F.6
  • 55
    • 0033551440 scopus 로고    scopus 로고
    • Assembly of Ab amyloid protofibrils: An in vitro model for a possible early event in Alzheimer's disease
    • Harper J.D., Wong S.S., Lieber C.M., Lansbury P.T. Assembly of Ab amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease. Biochemistry. 38:1999;8972-8980.
    • (1999) Biochemistry , vol.38 , pp. 8972-8980
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 56
    • 0028087275 scopus 로고
    • Atomic force microscopy produces faithful high-resolution images of protein surfaces in an aqueous environment
    • Karrasch S., Hegerl R., Hoh J.H., Baumeister W., Engel A. Atomic force microscopy produces faithful high-resolution images of protein surfaces in an aqueous environment. Proc. Natl. Acad. Sci. USA. 91:1993;836-838.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 836-838
    • Karrasch, S.1    Hegerl, R.2    Hoh, J.H.3    Baumeister, W.4    Engel, A.5
  • 57
    • 0029862834 scopus 로고    scopus 로고
    • Direct observation of protein secondary structure in gas vesicles by atomic force microscopy
    • McMaster T.J., Miles M.J., Walsby A.E. Direct observation of protein secondary structure in gas vesicles by atomic force microscopy. Biophys. J. 70:1996;2432-2436.
    • (1996) Biophys. J. , vol.70 , pp. 2432-2436
    • McMaster, T.J.1    Miles, M.J.2    Walsby, A.E.3
  • 58
    • 0141595787 scopus 로고    scopus 로고
    • Tapping-mode atomic microscopy produces faithful high-resolution images of protein surfaces
    • Möller C., Allen M., Elings V., Engel A., Müller D.J. Tapping-mode atomic microscopy produces faithful high-resolution images of protein surfaces. Biophys. J. 77:1999;1150-1158.
    • (1999) Biophys. J. , vol.77 , pp. 1150-1158
    • Möller, C.1    Allen, M.2    Elings, V.3    Engel, A.4    Müller, D.J.5
  • 61
    • 0031998544 scopus 로고    scopus 로고
    • Developments and perspectives of scanning probe microscopy (SPM) on organic materials systems
    • Jandt K.D. Developments and perspectives of scanning probe microscopy (SPM) on organic materials systems. Materials Sci. Engin. R21:1998;221-295.
    • (1998) Materials Sci. Engin. , vol.21 , pp. 221-295
    • Jandt, K.D.1
  • 63
    • 0016904284 scopus 로고
    • Interfacial enzyme kinetics of lipolysis
    • Mullinis L.J, Hagins W.A, Stryer L, Newton C.
    • Verger R., de Haas G.H. Interfacial enzyme kinetics of lipolysis. Mullinis L.J, Hagins W.A, Stryer L, Newton C. Ann. Rev. Biophys. Bioengin. 5:1976;77-117.
    • (1976) Ann. Rev. Biophys. Bioengin. , vol.5 , pp. 77-117
    • Verger, R.1    De Haas, G.H.2
  • 64
    • 0342890045 scopus 로고    scopus 로고
    • Preparation techniques for the observation of native biological systems with the atomic force microscope
    • Muller D., Engel A., Amrein M. Preparation techniques for the observation of native biological systems with the atomic force microscope. Biosensors Bioelectr. 12:1997;867-877.
    • (1997) Biosensors Bioelectr. , vol.12 , pp. 867-877
    • Muller, D.1    Engel, A.2    Amrein, M.3
  • 66
  • 67
    • 0003148667 scopus 로고    scopus 로고
    • Scanning probe microscopy (STM/AFM) and applications in biology
    • Li M.Q. Scanning probe microscopy (STM/AFM) and applications in biology. Appl. Phys. A. 68:1999;255-258.
    • (1999) Appl. Phys. A. , vol.68 , pp. 255-258
    • Li, M.Q.1
  • 68
    • 0001584583 scopus 로고    scopus 로고
    • Guidelines for the achievement of true atomic resolution with noncontact AFM
    • Morita S., Sugawara Y. Guidelines for the achievement of true atomic resolution with noncontact AFM. Appl. Surf. Sci. 140:1999;406-410.
    • (1999) Appl. Surf. Sci. , vol.140 , pp. 406-410
    • Morita, S.1    Sugawara, Y.2
  • 69
    • 11944250146 scopus 로고
    • Atomic force microscopy
    • Rugar D., Hansma P.K. Atomic force microscopy. Phys. Today. 43:1990;23-30.
    • (1990) Phys. Today , vol.43 , pp. 23-30
    • Rugar, D.1    Hansma, P.K.2
  • 70
    • 0027426465 scopus 로고
    • Promises and problems of biological atomic force microscopy
    • Yang J., Tamm L.K., Somlyo A.P., Shao Z. Promises and problems of biological atomic force microscopy. J. Microsc. 171:1993;183-198.
    • (1993) J. Microsc. , vol.171 , pp. 183-198
    • Yang, J.1    Tamm, L.K.2    Somlyo, A.P.3    Shao, Z.4
  • 71
    • 0033894687 scopus 로고    scopus 로고
    • Formation of supported phospholipid bilayers from unilamellar vesicles investigated by atomic force microscopy
    • Reviakine I., Brisson A. Formation of supported phospholipid bilayers from unilamellar vesicles investigated by atomic force microscopy. Langmuir. 16:2000;1473-1477.
    • (2000) Langmuir , vol.16 , pp. 1473-1477
    • Reviakine, I.1    Brisson, A.2
  • 72
    • 0021947327 scopus 로고
    • Supported phospholipid bilayers
    • Tamm L.K., McConnell H.M. Supported phospholipid bilayers. Biophys. J. 47:1985;105-113.
    • (1985) Biophys. J. , vol.47 , pp. 105-113
    • Tamm, L.K.1    McConnell, H.M.2
  • 73
    • 0033880358 scopus 로고    scopus 로고
    • 2+ on the morphology of mixed DPPC-DOPS supported phospholipid bilayers
    • 2+ on the morphology of mixed DPPC-DOPS supported phospholipid bilayers. Langmuir. 16:2000;1806-1815.
    • (2000) Langmuir , vol.16 , pp. 1806-1815
    • Reviakine, I.1    Brisson, A.2
  • 76
    • 0000227825 scopus 로고
    • Influence of cations, alkane chain length and substrate on molecular order of Langmuir-Blogett films
    • Schwartz D.K., Viswanathan R., Garnaes J., Zasadzinski J.A. Influence of cations, alkane chain length and substrate on molecular order of Langmuir-Blogett films. J. Am. Chem. Soc. 115:1993;7374-7380.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7374-7380
    • Schwartz, D.K.1    Viswanathan, R.2    Garnaes, J.3    Zasadzinski, J.A.4
  • 78
    • 0027114177 scopus 로고
    • Domain boundaries and buckling superstructures in Langmuir Blodgett films
    • Garnaes J., Schwartz D.K., Viswanathan R., Zasadzinski J.A. Domain boundaries and buckling superstructures in Langmuir Blodgett films. Nature. 357:1992;54-57.
    • (1992) Nature , vol.357 , pp. 54-57
    • Garnaes, J.1    Schwartz, D.K.2    Viswanathan, R.3    Zasadzinski, J.A.4
  • 79
    • 0028842124 scopus 로고
    • The structure and stability of phospholipid bilayers by atomic force microscopy
    • Hui S.W., Viswanathan R., Zasadzinski J.A., Israelachvili N. The structure and stability of phospholipid bilayers by atomic force microscopy. Biophys. J. 68:1995;171-178.
    • (1995) Biophys. J. , vol.68 , pp. 171-178
    • Hui, S.W.1    Viswanathan, R.2    Zasadzinski, J.A.3    Israelachvili, N.4
  • 81
    • 0029021712 scopus 로고
    • Progress in high resolution atomic force microscopy
    • Shao Z., Yang J. Progress in high resolution atomic force microscopy. Q. Rev. Biophys. 28:1995;195-251.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 195-251
    • Shao, Z.1    Yang, J.2
  • 86
    • 0032139532 scopus 로고    scopus 로고
    • Enzyme-assisted nano-scale lithography in lipid membranes
    • Clausen-Schaumann H., Grandbois M., Gaub H.E. Enzyme-assisted nano-scale lithography in lipid membranes. Adv. Mat. 10:1998;949-951.
    • (1998) Adv. Mat. , vol.10 , pp. 949-951
    • Clausen-Schaumann, H.1    Grandbois, M.2    Gaub, H.E.3
  • 90
    • 0035006294 scopus 로고    scopus 로고
    • Novel methods for studying lipids and lipases and their mutual interaction at interfaces. Part II. Surface sensitive synchrotron X-ray scattering
    • Jensen T.R., Balashev K., Bjørnholm T., Kjaer K. Novel methods for studying lipids and lipases and their mutual interaction at interfaces. Part II. Surface sensitive synchrotron X-ray scattering. Biochimie. 83:2001;399-408.
    • (2001) Biochimie , vol.83 , pp. 399-408
    • Jensen, T.R.1    Balashev, K.2    Bjørnholm, T.3    Kjaer, K.4


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