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Volumn 46, Issue 45, 2007, Pages 13089-13100

Effects of lipid phase transition and membrane surface charge on the interfacial activation of phospholipase A2

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; ENZYME ACTIVITY; FLUIDITY; MEMBRANES; PHOSPHOLIPIDS; SURFACE CHEMISTRY;

EID: 36048960156     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7015102     Document Type: Article
Times cited : (30)

References (44)
  • 4
    • 0034739443 scopus 로고    scopus 로고
    • Do membrane-bound enzymes access their substrates from the membrane or aqueous phase: Interfacial versus non-interfacial enzymes
    • Gelb, M. H., Min, J.-H., and Jain, M. K. (2000) Do membrane-bound enzymes access their substrates from the membrane or aqueous phase: interfacial versus non-interfacial enzymes, Biochim. Biophys. Acta 1488, 20-27.
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 20-27
    • Gelb, M.H.1    Min, J.-H.2    Jain, M.K.3
  • 5
    • 0040182776 scopus 로고    scopus 로고
    • 2 with phosphatidylcholine- phosphatidylglycerol mixed lipids
    • 2 with phosphatidylcholine- phosphatidylglycerol mixed lipids, Biochemistry 39, 9623-9631.
    • (2000) Biochemistry , vol.39 , pp. 9623-9631
    • Gadd, M.E.1    Biltonen, R.L.2
  • 7
    • 33644542722 scopus 로고    scopus 로고
    • 2: A differential role for electrostatics
    • 2: A differential role for electrostatics, Biochemistry 45, 2584-2598.
    • (2006) Biochemistry , vol.45 , pp. 2584-2598
    • Diraviyam, K.1    Murray, D.2
  • 9
    • 0025783513 scopus 로고
    • 2 from pancreas and venom using a continuous fluorescence displacement assay
    • 2 from pancreas and venom using a continuous fluorescence displacement assay, Biochem. J. 278, 843-848.
    • (1991) Biochem. J , vol.278 , pp. 843-848
    • Kinkaid, A.1    Wilton, D.C.2
  • 19
    • 0029866857 scopus 로고    scopus 로고
    • 2 activity: Interactions among temperature, diacylglycerol, lysolecithin, palmitic acid, and dipalmitoylphosphatidylcholine
    • 2 activity: interactions among temperature, diacylglycerol, lysolecithin, palmitic acid, and dipalmitoylphosphatidylcholine, Biochemistry 35, 4945-4955.
    • (1996) Biochemistry , vol.35 , pp. 4945-4955
    • Bell, J.D.1    Burnside, M.2    Owen, J.A.3    Royall, M.L.4    Baker, M.L.5
  • 26
    • 23644451829 scopus 로고    scopus 로고
    • Positioning membrane proteins by novel protein engineering and biophysical approaches
    • Tatulian, S. A., Qin, S., Pande, A. H., and He, X. (2005) Positioning membrane proteins by novel protein engineering and biophysical approaches, J. Mol. Biol. 351, 939-947.
    • (2005) J. Mol. Biol , vol.351 , pp. 939-947
    • Tatulian, S.A.1    Qin, S.2    Pande, A.H.3    He, X.4
  • 28
    • 7044269246 scopus 로고    scopus 로고
    • 2 determines productive-mode orientation of the enzyme at the membrane surface
    • 2 determines productive-mode orientation of the enzyme at the membrane surface, J. Mol. Biol. 344, 71-89.
    • (2004) J. Mol. Biol , vol.344 , pp. 71-89
    • Qin, S.1    Pande, A.H.2    Nemec, K.N.3    Tatulian, S.A.4
  • 29
    • 3142643268 scopus 로고    scopus 로고
    • Laurdan and prodan as polarity-sensitive fluorescent membrane probes
    • Parasassi, T., Krasnowska, E. K., Bagatolli, L., and Gratton, E. (1998) Laurdan and prodan as polarity-sensitive fluorescent membrane probes, J. Fluoresc. 8, 365-373.
    • (1998) J. Fluoresc , vol.8 , pp. 365-373
    • Parasassi, T.1    Krasnowska, E.K.2    Bagatolli, L.3    Gratton, E.4
  • 30
    • 33745448224 scopus 로고    scopus 로고
    • Laurdan in fluid bilayers: Position and structural sensitivity
    • De Vequi-Suplicy, C. C., Benatti, C. R., and Lamy, M. T. (2006) Laurdan in fluid bilayers: Position and structural sensitivity, J. Fluoresc. 16, 431-439.
    • (2006) J. Fluoresc , vol.16 , pp. 431-439
    • De Vequi-Suplicy, C.C.1    Benatti, C.R.2    Lamy, M.T.3
  • 31
    • 0031005647 scopus 로고    scopus 로고
    • Distribution analysis of depth-dependent fluorescence quenching in membranes: A practical guide
    • Ladokhin, A. S. (1997) Distribution analysis of depth-dependent fluorescence quenching in membranes: a practical guide, Methods Enzymol. 278, 462-473.
    • (1997) Methods Enzymol , vol.278 , pp. 462-473
    • Ladokhin, A.S.1
  • 32
    • 35848955007 scopus 로고    scopus 로고
    • Measuring the depth of amino acid residues in membrane-inserted peptides by fluorescence quenching
    • London, E., and Ladokhin, A. S. (2002) Measuring the depth of amino acid residues in membrane-inserted peptides by fluorescence quenching, Curr. Top. Membr. 52, 89-115.
    • (2002) Curr. Top. Membr , vol.52 , pp. 89-115
    • London, E.1    Ladokhin, A.S.2
  • 34
    • 0023111150 scopus 로고
    • Determination of the depth of bromine atoms in bilayers formed from bromolipid probes
    • McIntosh, T. J., and Holloway, P. W. (1987) Determination of the depth of bromine atoms in bilayers formed from bromolipid probes, Biochemistry 26, 1783-1788.
    • (1987) Biochemistry , vol.26 , pp. 1783-1788
    • McIntosh, T.J.1    Holloway, P.W.2
  • 37
    • 0021396114 scopus 로고
    • The effects of water-soluble solutes on the phase transitions of phospholipids
    • Sturtevant, J. M. (1984) The effects of water-soluble solutes on the phase transitions of phospholipids, Proc. Natl. Acad. Sci. U.S.A. 81, 1398-1400.
    • (1984) Proc. Natl. Acad. Sci. U.S.A , vol.81 , pp. 1398-1400
    • Sturtevant, J.M.1
  • 38
    • 0004224163 scopus 로고
    • Cevc, G, Ed, Marcel Dekker, New York
    • Cevc, G., Ed. (1993) Phospholipids Handbook, Marcel Dekker, New York.
    • (1993) Phospholipids Handbook
  • 40
    • 0002940760 scopus 로고
    • Ionization and ion binding
    • Cevc, G, Ed, pp, Marcel Dekker, New York
    • Tatulian, S. A. (1993) Ionization and ion binding, in Phospholipids Handbook (Cevc, G., Ed.) pp 511-552, Marcel Dekker, New York.
    • (1993) Phospholipids Handbook , pp. 511-552
    • Tatulian, S.A.1
  • 41
    • 0034667871 scopus 로고    scopus 로고
    • How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?
    • Ladokhin, A. S., Jayasinghe, S., and White, S. H. (2000) How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?, Anal. Biochem. 285, 235-245.
    • (2000) Anal. Biochem , vol.285 , pp. 235-245
    • Ladokhin, A.S.1    Jayasinghe, S.2    White, S.H.3
  • 43
    • 33845374715 scopus 로고
    • Microviscosity measurements of phospholipid bilayers using fluorescent dyes that undergo torsional relaxation
    • Kung, C. E., and Reed, J. K. (1986) Microviscosity measurements of phospholipid bilayers using fluorescent dyes that undergo torsional relaxation, Biochemistry 25, 6114-6121.
    • (1986) Biochemistry , vol.25 , pp. 6114-6121
    • Kung, C.E.1    Reed, J.K.2
  • 44
    • 0018910496 scopus 로고
    • 2 on unmodified phosphatidylcholine bilayers: Organizational defects are preferred sites of action
    • 2 on unmodified phosphatidylcholine bilayers: organizational defects are preferred sites of action, J. Membr. Biol. 55, 113-121.
    • (1980) J. Membr. Biol , vol.55 , pp. 113-121
    • Upreti, G.C.1    Jain, M.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.