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Volumn 13, Issue 6, 1997, Pages 828-836

Refolding of carbonic anhydrase assisted by 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine liposomes

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CATALYST ACTIVITY; THERMAL EFFECTS;

EID: 0031278523     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp970104m     Document Type: Article
Times cited : (68)

References (38)
  • 1
    • 0038259804 scopus 로고    scopus 로고
    • Interaction of native and partially folded conformations of α-lactalubumin with lipid bilayers: Characterization of two membrane-bound states
    • Banuelos, S.; Muga, A. Interaction of native and partially folded conformations of α-lactalubumin with lipid bilayers: characterization of two membrane-bound states. FEBS Lett. 1996, 386, 21-25.
    • (1996) FEBS Lett. , vol.386 , pp. 21-25
    • Banuelos, S.1    Muga, A.2
  • 2
    • 0023710642 scopus 로고
    • The molten globule' state in involved in the translocation of protein across membrane?
    • Bychkova, V. E.; Pain, R. H.; Ptitsyn, O. B. The molten globule' state in involved in the translocation of protein across membrane? FEBS Lett. 1988, 238 (2), 231-234.
    • (1988) FEBS Lett. , vol.238 , Issue.2 , pp. 231-234
    • Bychkova, V.E.1    Pain, R.H.2    Ptitsyn, O.B.3
  • 3
    • 0344311712 scopus 로고
    • Liposomes as drug delivery
    • Diagnostic, C.; Potential, O. Liposomes as drug delivery. Drugs 1993, 45 (1), 15-28.
    • (1993) Drugs , vol.45 , Issue.1 , pp. 15-28
    • Diagnostic, C.1    Potential, O.2
  • 4
    • 0030586394 scopus 로고    scopus 로고
    • A 1H nuclear magnetic resonance method for investigating the phospholipase D-catalyzed hydrolysis of phosphatidylcholine
    • Dorovska-Taran, V.; Wick, R.; Walde, P. A 1H nuclear magnetic resonance method for investigating the phospholipase D-catalyzed hydrolysis of phosphatidylcholine. Anal. Biochem. 1996, 240, 37-47.
    • (1996) Anal. Biochem. , vol.240 , pp. 37-47
    • Dorovska-Taran, V.1    Wick, R.2    Walde, P.3
  • 6
    • 0022999335 scopus 로고
    • Target-sensitive immunoliposomes: Preparation and characterization
    • Ho, R. J.; Rouse, B. T.; Huang, L. Target-sensitive immunoliposomes: preparation and characterization. Biochemistry 1986, 25, 5500-5506.
    • (1986) Biochemistry , vol.25 , pp. 5500-5506
    • Ho, R.J.1    Rouse, B.T.2    Huang, L.3
  • 7
    • 0013347430 scopus 로고
    • Eine Methode zur routinemässigen bestimmung des lipidphosphors und der phosphatide
    • Hoeflmayr, J.; Fried, R. Eine Methode zur routinemässigen bestimmung des lipidphosphors und der phosphatide. Med. Ernaehr. 1966, 7, 9-10.
    • (1966) Med. Ernaehr. , vol.7 , pp. 9-10
    • Hoeflmayr, J.1    Fried, R.2
  • 8
    • 0025736080 scopus 로고
    • Possibility of heat sterilization of liposomes
    • Kikuchi, H.; Carlsson, A.; Yachi, K.; Hirota, S. Possibility of heat sterilization of liposomes. Chem. Pharm. Bull. 1991, 39 (4), 1018-1022.
    • (1991) Chem. Pharm. Bull. , vol.39 , Issue.4 , pp. 1018-1022
    • Kikuchi, H.1    Carlsson, A.2    Yachi, K.3    Hirota, S.4
  • 9
    • 85010168293 scopus 로고
    • Evaluation of surface hydrophobicities during refolding process of carbonic anhydrase
    • Kuboi, R.; Yano, K.; Tanaka, H.; Komasawa, I. Evaluation of surface hydrophobicities during refolding process of carbonic anhydrase. J. Chem. Eng. Jpn. 1993, 26, 286-290.
    • (1993) J. Chem. Eng. Jpn. , vol.26 , pp. 286-290
    • Kuboi, R.1    Yano, K.2    Tanaka, H.3    Komasawa, I.4
  • 10
    • 0001817888 scopus 로고
    • Evaluation of surface potentials and partitioning of proteins in aqueous two-phase systems
    • Kuboi, R.; Yano, K.; Komasawa, I. Evaluation of surface potentials and partitioning of proteins in aqueous two-phase systems. Solvent Extr. Res. Dev., Jpn. 1994, 1, 42-52.
    • (1994) Solvent Extr. Res. Dev., Jpn. , vol.1 , pp. 42-52
    • Kuboi, R.1    Yano, K.2    Komasawa, I.3
  • 11
    • 0029104840 scopus 로고
    • Purification process for heat shock proteins using aqueous two-phase systems and PEG fractional precipitation
    • Kuboi, R.; Hasegawa, T.; Yano, K.; Komasawa, I. Purification process for heat shock proteins using aqueous two-phase systems and PEG fractional precipitation. J. Chem. Eng. Jpn. 1995, 28, 797-802.
    • (1995) J. Chem. Eng. Jpn. , vol.28 , pp. 797-802
    • Kuboi, R.1    Hasegawa, T.2    Yano, K.3    Komasawa, I.4
  • 12
    • 0342563780 scopus 로고
    • Catalytic hydrolysis of phenyl esters in aqueous didodecyldimethylammonium vesicles: Remarkable rate difference between intra- and intervesicle reactions
    • Kunitake, T.; Sakamoto, T. Catalytic hydrolysis of phenyl esters in aqueous didodecyldimethylammonium vesicles: remarkable rate difference between intra-and intervesicle reactions. J. Am. Chem. Soc. 1978, 100, 4615-4617.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 4615-4617
    • Kunitake, T.1    Sakamoto, T.2
  • 13
    • 0027495558 scopus 로고
    • Use of Fluorescent probes to monitor molecular order and motions within liposome bilayers
    • Lentz, B. R. Use of Fluorescent probes to monitor molecular order and motions within liposome bilayers. Chem. Phys. Lipids 1993, 64, 99-116.
    • (1993) Chem. Phys. Lipids , vol.64 , pp. 99-116
    • Lentz, B.R.1
  • 14
    • 0024290906 scopus 로고
    • Temperature, pressure and cholesterol effects on bilayer fluidity; a comparison of pyrene eximer/monomer ratios with the steady-state fluorescence polarization of diphenylhexatriene in liposomes and microsomes
    • MacDonald, A. G.; Wahle, K. W. J.; Cossines, A. R.; Behan, M. K. Temperature, pressure and cholesterol effects on bilayer fluidity; a comparison of pyrene eximer/monomer ratios with the steady-state fluorescence polarization of diphenylhexatriene in liposomes and microsomes. Biochim. Biophys. Acta 1988, 938, 231-242.
    • (1988) Biochim. Biophys. Acta , vol.938 , pp. 231-242
    • MacDonald, A.G.1    Wahle, K.W.J.2    Cossines, A.R.3    Behan, M.K.4
  • 16
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of GroEL through a 'molten-globule'-like intermediate
    • Martin, J.; Langer, T.; Botena, R.; Scramel, A.; Howich, A. L.; Hartl, F.-U. Chaperonin-mediated protein folding at the surface of GroEL through a 'molten-globule'-like intermediate. Nature 1991, 352, 36-42.
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Botena, R.3    Scramel, A.4    Howich, A.L.5    Hartl, F.-U.6
  • 17
    • 0025877054 scopus 로고
    • Apocytochrome c interaction with phospholipid membranes stidied by fourier-transform infrared spectroscopy
    • Muga, A.; Mantsch, H. H.; Surewicz, W. K. Apocytochrome c interaction with phospholipid membranes stidied by fourier-transform infrared spectroscopy. Biochemistry 1991, 30, 2629-2635.
    • (1991) Biochemistry , vol.30 , pp. 2629-2635
    • Muga, A.1    Mantsch, H.H.2    Surewicz, W.K.3
  • 18
    • 0019134303 scopus 로고
    • Freezing in a propane jet and its application in freeze-fracturing
    • Müller, M.; Meister, N.; Moor, H. Freezing in a propane jet and its application in freeze-fracturing. Mikroskopie 1980, 36, 129-140.
    • (1980) Mikroskopie , vol.36 , pp. 129-140
    • Müller, M.1    Meister, N.2    Moor, H.3
  • 20
    • 0015217634 scopus 로고
    • Solubility of amino acids and two glycine in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity Scale
    • Nozaki, Y.; Tanford, C. Solubility of amino acids and two glycine in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity Scale. J. Biol. Chem. 1971, 246, 2211-2217.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2211-2217
    • Nozaki, Y.1    Tanford, C.2
  • 21
  • 23
    • 0014062860 scopus 로고
    • The catalytic versatility of erythrocyte carbonic anhydrase. III. Kinetic studies of the enzyme-catalyzed hydrolysis of p-nitrophenyl acetate
    • Pocker, Y.; Stone, J. T. The catalytic versatility of erythrocyte carbonic anhydrase. III. Kinetic studies of the enzyme-catalyzed hydrolysis of p-nitrophenyl acetate. Biochemistry 1967, 6, 668-678.
    • (1967) Biochemistry , vol.6 , pp. 668-678
    • Pocker, Y.1    Stone, J.T.2
  • 24
    • 0025212107 scopus 로고
    • Evidence for a molten globule state as a general intermediate in protein folding
    • Ptitsyn, O. B.; Pain, R. H.; Semisotnov, G. V.; Zerovnik, E.; Razgulyaev, O. I. Evidence for a molten globule state as a general intermediate in protein folding. FEBS Lett. 1990, 262 (1), 20-24.
    • (1990) FEBS Lett. , vol.262 , Issue.1 , pp. 20-24
    • Ptitsyn, O.B.1    Pain, R.H.2    Semisotnov, G.V.3    Zerovnik, E.4    Razgulyaev, O.I.5
  • 26
    • 0023051872 scopus 로고
    • An unfolding story of protein translocation
    • Rothman, J. E.; Kornberg, R. D. An unfolding story of protein translocation. Nature 1986, 322, 209-210.
    • (1986) Nature , vol.322 , pp. 209-210
    • Rothman, J.E.1    Kornberg, R.D.2
  • 27
    • 0026060897 scopus 로고
    • Influence of surface hydrophobicity of liposomes on their interaction with plasma protein and clearance from the circulation: Studies with poly(ethylene glycol)-coated vesicles
    • Senior, J.; Delgado, C.; Fisher, D.; Tilcook, C.; Gregoriadis, G. Influence of surface hydrophobicity of liposomes on their interaction with plasma protein and clearance from the circulation: studies with poly(ethylene glycol)-coated vesicles. Biochim. Biophys. Acta 1991, 1062, 77-82.
    • (1991) Biochim. Biophys. Acta , vol.1062 , pp. 77-82
    • Senior, J.1    Delgado, C.2    Fisher, D.3    Tilcook, C.4    Gregoriadis, G.5
  • 28
    • 0026770209 scopus 로고
    • Refolding and oriented insertion of membrane protein into a lipid bilayer
    • Surrey, T.; Jähnig, F. Refolding and oriented insertion of membrane protein into a lipid bilayer. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 7457-7461.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 7457-7461
    • Surrey, T.1    Jähnig, F.2
  • 29
    • 0028930164 scopus 로고
    • Effect of cholesterol, fatty acyl chain composition, and bilayer curvature on the interaction of cytochrome b5 with liposomes of phosphatidylcholine
    • Taylor, K. M. P.; Roseman, M. A. Effect of cholesterol, fatty acyl chain composition, and bilayer curvature on the interaction of cytochrome b5 with liposomes of phosphatidylcholine. Biochemistry 1995, 34, 3841-3850.
    • (1995) Biochemistry , vol.34 , pp. 3841-3850
    • Taylor, K.M.P.1    Roseman, M.A.2
  • 30
    • 84961484174 scopus 로고
    • Quantitative determination of total urinary protein utilizing the principle of coomassie brilliant blue G250 binding to protein
    • Thomas, L.; Winckelmann, M.; Michaelis, H. C.; Walb, D. J. Quantitative determination of total urinary protein utilizing the principle of coomassie brilliant blue G250 binding to protein. Clin. Chem. Clin. Biochem. 1981, 19, (4), 203-208.
    • (1981) Clin. Chem. Clin. Biochem. , vol.19 , Issue.4 , pp. 203-208
    • Thomas, L.1    Winckelmann, M.2    Michaelis, H.C.3    Walb, D.J.4
  • 32
    • 85008135835 scopus 로고
    • Characterization of surface properties of heat shock proteins for the separation using aqueous two-phase systems
    • Yano, K; Hasegawa, T.; Kuboi, R.; Komasawa, I.; Tsuchido, T. Characterization of surface properties of heat shock proteins for the separation using aqueous two-phase systems. J. Chem. Eng. Jpn. 1994, 27, 808-814.
    • (1994) J. Chem. Eng. Jpn. , vol.27 , pp. 808-814
    • Yano, K.1    Hasegawa, T.2    Kuboi, R.3    Komasawa, I.4    Tsuchido, T.5
  • 33
    • 0018952681 scopus 로고
    • Kinetic Characterization of Liposomes
    • Yotsuyanagi, T.; Ikeda, K. Kinetic Characterization of Liposomes. J. Pharm. Sci. 1980, 69 (6), 745-746.
    • (1980) J. Pharm. Sci. , vol.69 , Issue.6 , pp. 745-746
    • Yotsuyanagi, T.1    Ikeda, K.2
  • 34
    • 0028260023 scopus 로고
    • Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
    • Zanh, R.; Spizfaden, C.; Ottiger, M.; Wuthrich, K.; Pluckthun, A. Destabilization of the complete protein secondary structure on binding to the chaperone GroEL. Nature 1994, 368, 261-265.
    • (1994) Nature , vol.368 , pp. 261-265
    • Zanh, R.1    Spizfaden, C.2    Ottiger, M.3    Wuthrich, K.4    Pluckthun, A.5
  • 35
    • 0027067992 scopus 로고
    • Cardiolipin liposomes sequester a reactivatable partially folded rhodanese intermediate
    • Zardeneta, G.; Horowitz, P. M. Cardiolipin liposomes sequester a reactivatable partially folded rhodanese intermediate. J. Biochem. 1992, 210, 831-837.
    • (1992) J. Biochem. , vol.210 , pp. 831-837
    • Zardeneta, G.1    Horowitz, P.M.2
  • 36
    • 0028348944 scopus 로고
    • Protein refolding at high concentration using detergent/phospholipid mixtures
    • Zardeneta, G.; Horowitz, P. M. Protein refolding at high concentration using detergent/phospholipid mixtures. Anal. Biochem. 1994a, 218, 392-398.
    • (1994) Anal. Biochem. , vol.218 , pp. 392-398
    • Zardeneta, G.1    Horowitz, P.M.2
  • 37
    • 0028152452 scopus 로고
    • Detergent, Liposome, and micelle-assisted protein refolding
    • Zardeneta, G.; Horowitz, P. M. Detergent, Liposome, and micelle-assisted protein refolding. Anal. Biochem. 1994b, 223, 1-6.
    • (1994) Anal. Biochem. , vol.223 , pp. 1-6
    • Zardeneta, G.1    Horowitz, P.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.