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Volumn 13, Issue 2, 1996, Pages 265-271

Interaction between superoxide dismutase and dipalmitoylphosphotidylglycerol bilayers: A Fourier transform infrared (FT-IR) spectroscopic study

Author keywords

Conformation; Curve fitting; FT IR; Lipid membranes; Superoxide dismutase; Thermal stability

Indexed keywords

ANTIOXIDANT; DIPALMITOYLPHOSPHATIDYLGLYCEROL; SUPEROXIDE DISMUTASE;

EID: 0030030962     PISSN: 07248741     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1016099232745     Document Type: Article
Times cited : (11)

References (23)
  • 1
    • 0020427486 scopus 로고
    • Biology of Disease: Free Radicals and Tissue Injury
    • B. A. Freeman. Biology of Disease: Free Radicals and Tissue Injury. Lab. Invest. 47:412-426 (1982).
    • (1982) Lab. Invest. , vol.47 , pp. 412-426
    • Freeman, B.A.1
  • 2
    • 84988180646 scopus 로고
    • Exogenous Control of Pulmonary Antioxidant Defenses
    • S. I. Said (ed.), Futura, New York
    • R. R. Baker and B. A. Freeman. Exogenous Control of Pulmonary Antioxidant Defenses. In S. I. Said (ed.), The Pulmonary Circulation and Acute Lung Injury, Futura, New York, 1991, pp 473-496.
    • (1991) The Pulmonary Circulation and Acute Lung Injury , pp. 473-496
    • Baker, R.R.1    Freeman, B.A.2
  • 3
    • 0027354746 scopus 로고
    • Oxidant Injury to the Alveolar Epithelium: Biochemical and Pharmacologie Studies
    • B. A. Freeman, P. C. Panus, S. Matalon, B. J. Buckley, and R. R. Baker. Oxidant Injury to the Alveolar Epithelium: Biochemical and Pharmacologie Studies. Research Report 54:1-39 (1993).
    • (1993) Research Report , vol.54 , pp. 1-39
    • Freeman, B.A.1    Panus, P.C.2    Matalon, S.3    Buckley, B.J.4    Baker, R.R.5
  • 5
    • 0001174425 scopus 로고
    • Clinical Use of Superoxide Dismutase and Possible Pharmacological Approaches
    • A. P. Autor (ed.), Academic Press, New York
    • A. M. Michelson. Clinical Use of Superoxide Dismutase and Possible Pharmacological Approaches. In A. P. Autor (ed.), Pathology of Oxygen Radicals, Academic Press, New York, 1982, pp. 277-302.
    • (1982) Pathology of Oxygen Radicals , pp. 277-302
    • Michelson, A.M.1
  • 6
    • 0003870684 scopus 로고
    • Liposome-Entrapped Superoxide Dismutase: In Vitro and in Vivo Effects
    • G. Gregoriadis (ed.), Wiley, New York
    • P. C. Panus and B. A. Freeman. Liposome-Entrapped Superoxide Dismutase: in Vitro and in Vivo Effects. In G. Gregoriadis (ed.), Liposomes as Drug Carriers., Wiley, New York, 1988, pp 473-482.
    • (1988) Liposomes as Drug Carriers , pp. 473-482
    • Panus, P.C.1    Freeman, B.A.2
  • 7
    • 0021795717 scopus 로고
    • Modulation of Oxidant Lung Injury by Using Liposome-Entrapped Superoxide Dismutase and Catalase
    • B. A. Freeman, J. F. Turrens, Z. Mirza, J. D. Crapo, and S. L. Young. Modulation of Oxidant Lung Injury by Using Liposome-Entrapped Superoxide Dismutase and Catalase. Fed. Proc. 44:2591-2595 (1985).
    • (1985) Fed. Proc. , vol.44 , pp. 2591-2595
    • Freeman, B.A.1    Turrens, J.F.2    Mirza, Z.3    Crapo, J.D.4    Young, S.L.5
  • 9
    • 0029014955 scopus 로고
    • Protein Location in Liposomes, a Lipid Carrier: A Prediction by Differential Scanning Calorimetry
    • Y.-L. Lo and Y. E. Rahman. Protein Location in Liposomes, A Lipid Carrier: A Prediction by Differential Scanning Calorimetry. J. Pharm. Sci. 84:805-814 (1995).
    • (1995) J. Pharm. Sci. , vol.84 , pp. 805-814
    • Lo, Y.-L.1    Rahman, Y.E.2
  • 10
    • 0027323183 scopus 로고
    • Secondary Structure and Temperature-Induced Unfolding and Refolding of Ribonuclease T1 in Aqueous Solution. A Fourier Transform Infrared Spectroscopic Study
    • H. Fabian, C. Schultz, D. Naumann, O. Landt, U. Hahn, and W. Saenger. Secondary Structure and Temperature-Induced Unfolding and Refolding of Ribonuclease T1 in Aqueous Solution. A Fourier Transform Infrared Spectroscopic Study. J. Mol. Biol. 232:967-981 (1993).
    • (1993) J. Mol. Biol. , vol.232 , pp. 967-981
    • Fabian, H.1    Schultz, C.2    Naumann, D.3    Landt, O.4    Hahn, U.5    Saenger, W.6
  • 11
    • 0023008334 scopus 로고
    • Vibrational Spectroscopy and Conformation of Peptides, Polypeptides and Proteins
    • S. Krimm and J. Bandekar. Vibrational Spectroscopy and Conformation of Peptides, Polypeptides and Proteins. Advan. Protein. Chem. 38:181-364 (1986).
    • (1986) Advan. Protein. Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 12
    • 0023837785 scopus 로고
    • New Insight into Protein Secondary Structure from Resolution-Enhanced Infrared Spectra
    • W. W. Surewicz and H. H. Mantsch. New Insight into Protein Secondary Structure from Resolution-Enhanced Infrared Spectra. Biochim. Biophys. Acta 952:115-130 (1988).
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.W.1    Mantsch, H.H.2
  • 13
    • 0022691315 scopus 로고
    • Examination of the Secondary Structure on Proteins by Deconvoluted FTIR Spectra
    • D. M. Byler and H. Susi. Examination of the Secondary Structure on Proteins by Deconvoluted FTIR Spectra. Biopolymers 25:469-487 (1986).
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 14
    • 0024963566 scopus 로고
    • Structure of Cytochrome b5 in Solution by Fourier-Transform Infrared Spectroscopy
    • P. W. Holloway and H. H. Mantsch. Structure of Cytochrome b5 in Solution by Fourier-Transform Infrared Spectroscopy. Biochem. 28:931-935 (1989).
    • (1989) Biochem. , vol.28 , pp. 931-935
    • Holloway, P.W.1    Mantsch, H.H.2
  • 15
    • 0025841667 scopus 로고
    • Membrane Binding Induces Destabilization of Cytochrome c Structure
    • A. Muga, H. H. Mantsch, and W. K. Surewicz. Membrane Binding Induces Destabilization of Cytochrome c Structure. Biochem. 30:7219-7224 (1991).
    • (1991) Biochem. , vol.30 , pp. 7219-7224
    • Muga, A.1    Mantsch, H.H.2    Surewicz, W.K.3
  • 16
    • 0028349385 scopus 로고
    • Thermally Denatured Ribonuclease a Retains Secondary Structure As Shown by FTIR
    • S. Seshadri, K. A. Oberg, and A. L. Fink. Thermally Denatured Ribonuclease A Retains Secondary Structure As Shown by FTIR. Biochem. 33:1351-1355 (1994).
    • (1994) Biochem. , vol.33 , pp. 1351-1355
    • Seshadri, S.1    Oberg, K.A.2    Fink, A.L.3
  • 17
    • 0028916150 scopus 로고
    • Infrared Spectroscopic Studies of Lyophilization- and Temperature-induced Protein Aggregation
    • A. Dong, S. J. Prestrelski, S. D. Allison, J. F. Carpenter. Infrared Spectroscopic Studies of Lyophilization- and Temperature-induced Protein Aggregation. J. Pharm. Sci. 84:415-424 (1995).
    • (1995) J. Pharm. Sci. , vol.84 , pp. 415-424
    • Dong, A.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 18
    • 0019536747 scopus 로고
    • Infrared and Laser-Raman Spectroscopic Studies of Thermally-Induced Globular Protein Gels
    • A. H. Clark, D. H. P. Saunderson, and A. Suggett. Infrared and Laser-Raman Spectroscopic Studies of Thermally-Induced Globular Protein Gels. J. Pept. Protein Res. 17:353-364 (1981).
    • (1981) J. Pept. Protein Res. , vol.17 , pp. 353-364
    • Clark, A.H.1    Saunderson, D.H.P.2    Suggett, A.3
  • 20
    • 0028120538 scopus 로고
    • Impact of Point Mutations on the Structure and Thermal Stability of Ribonuclease T1 in Aqueous Solution Probed by Fourier Transform Infrared Spectroscopy
    • H. Fabian, C. Schultz, J. Backmann, U. Hahn, W. Saenger, H. H. Mantsch. Impact of Point Mutations on the Structure and Thermal Stability of Ribonuclease T1 in Aqueous Solution Probed by Fourier Transform Infrared Spectroscopy. Biochem. 33:10725-10730 (1994).
    • (1994) Biochem. , vol.33 , pp. 10725-10730
    • Fabian, H.1    Schultz, C.2    Backmann, J.3    Hahn, U.4    Saenger, W.5    Mantsch, H.H.6
  • 21
    • 0027354020 scopus 로고
    • Quantitative Studies of the Structure of Proteins in Solution by Fourier-Transform Infrared Spectroscopy
    • J. L. Arrondo, R. A. Muga, J. Castresana, F. M. Goni. Quantitative Studies of the Structure of Proteins in Solution by Fourier-Transform Infrared Spectroscopy. Prog. Biophy. Molecu. Biol. 59:23-56 (1993).
    • (1993) Prog. Biophy. Molecu. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.1    Muga, R.A.2    Castresana, J.3    Goni, F.M.4
  • 22
    • 0024503517 scopus 로고
    • Binding of a Tightly Folded Artificial Mitochondrial Precursor Protein to the Mitochondrial Outer Membrane Involves a Lipid-Mediated Conformational Change
    • T. Endo, M. Eilers, and G. Schatz. Binding of a Tightly Folded Artificial Mitochondrial Precursor Protein to the Mitochondrial Outer Membrane Involves a Lipid-Mediated Conformational Change. J. Biol. Chem. 264:2951-2956 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 2951-2956
    • Endo, T.1    Eilers, M.2    Schatz, G.3
  • 23
    • 0017701604 scopus 로고
    • Automatic Identification of Secondary Structure in Globular Proteins
    • M. Levitt and J. Greer. Automatic Identification of Secondary Structure in Globular Proteins. J. Mol. Biol. 114:181-239 (1977).
    • (1977) J. Mol. Biol. , vol.114 , pp. 181-239
    • Levitt, M.1    Greer, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.