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Volumn 100-101, Issue , 1998, Pages 387-391

Volatile anesthetics alter protein stability

Author keywords

Differential scanning calorimetry; Protein stability; Volatile anesthetics

Indexed keywords

BOVINE SERUM ALBUMIN; HALOTHANE; HUMAN SERUM ALBUMIN; INHALATION ANESTHETIC AGENT; LYSOZYME; MYOGLOBIN; PANCREATIC RIBONUCLEASE; RIBONUCLEASE A;

EID: 18144445863     PISSN: 03784274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-4274(98)00211-2     Document Type: Conference Paper
Times cited : (11)

References (12)
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    • Alifimoff, J.K.1    Miller, K.W.2
  • 2
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    • Why water-soluble, compact, globular proteins have similar specific enthalpies of unfolding at 110°C
    • Doig, A.J., Williams, D.H., 1992. Why water-soluble, compact, globular proteins have similar specific enthalpies of unfolding at 110°C. Biochemistry 31, 9371-9375.
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    • Doig, A.J.1    Williams, D.H.2
  • 4
    • 0029900543 scopus 로고    scopus 로고
    • Amino-acid resolution of halothane binding sites in serum albumin
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    • (1996) J. Biol. Chem. , vol.271 , pp. 15521-15526
    • Eckenhoff, R.G.1
  • 5
    • 0027283792 scopus 로고
    • Halothane binding to soluble proteins determined by photoaffinity labeling
    • Eckenhoff, R.G., Shuman, H., 1993. Halothane binding to soluble proteins determined by photoaffinity labeling. Anesthesiology 79, 96-106.
    • (1993) Anesthesiology , vol.79 , pp. 96-106
    • Eckenhoff, R.G.1    Shuman, H.2
  • 6
    • 0021211620 scopus 로고
    • Do general anaesthetics act by competitive binding to specific receptors?
    • Franks, N.P., Lieb, W.R., 1984. Do general anaesthetics act by competitive binding to specific receptors? Nature 310, 599-601.
    • (1984) Nature , vol.310 , pp. 599-601
    • Franks, N.P.1    Lieb, W.R.2
  • 7
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    • Thermal stability of fatty acid-serum albumin complexes studied by differential scanning calorimetry
    • Gumpen, S., Hegg, P.O., Martens, H., 1979. Thermal stability of fatty acid-serum albumin complexes studied by differential scanning calorimetry. Biochim. Biophys. Acta 574, 189-196.
    • (1979) Biochim. Biophys. Acta , vol.574 , pp. 189-196
    • Gumpen, S.1    Hegg, P.O.2    Martens, H.3
  • 8
    • 0029122365 scopus 로고
    • Binding of halothane to serum albumin demonstrated using tryptophan fluorescence
    • Johansson, J.S., Eckenhoff, R.G., Dutton, P.L., 1995. Binding of halothane to serum albumin demonstrated using tryptophan fluorescence. Anesthesiology 83, 316-324.
    • (1995) Anesthesiology , vol.83 , pp. 316-324
    • Johansson, J.S.1    Eckenhoff, R.G.2    Dutton, P.L.3
  • 9
    • 0028845120 scopus 로고
    • Precise scanning calorimeter for studying thermal properties of biological macromolecules in dilute solution
    • Privalov, G., Kavina, V., Freire, E., Privalov, P.L., 1995. Precise scanning calorimeter for studying thermal properties of biological macromolecules in dilute solution. Anal. Biochem. 232, 79-85.
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    • Privalov, G.1    Kavina, V.2    Freire, E.3    Privalov, P.L.4
  • 10
    • 0026734102 scopus 로고
    • Two-dimensional differential scanning calorimetry: Simultaneous resolution of intrinsic protein structural energetics and ligand binding interactions by global linkage analysis
    • Straume, M., Freire, E., 1992. Two-dimensional differential scanning calorimetry: simultaneous resolution of intrinsic protein structural energetics and ligand binding interactions by global linkage analysis. Anal. Biochem. 203, 259-268.
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  • 11
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    • Kinetic and thermodynamic aspects of the mechanism of general anesthesia in a model system of firefly luminescence in vitro
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.