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Volumn 62, Issue 6, 1996, Pages 933-937

Studies on Thermal Denaturation of Fish Apomyoglobins using Differential Scanning Calorimetry, Circular Dichroism, and Fluorescence

Author keywords

Circular dichroism; Differential scanning calorimetry; Myoglobin; Protein stability; Thermal denaturation; Tryptophan fluorescence

Indexed keywords


EID: 0342382548     PISSN: 09199268     EISSN: None     Source Type: Journal    
DOI: 10.2331/fishsci.62.933     Document Type: Article
Times cited : (13)

References (23)
  • 2
    • 0025616115 scopus 로고
    • Characterization of hydrophobic cores in apomyoglobin: A proton NMR spectroscopy study
    • M. J. Cocco and J. T. J. Lecomte: Characterization of hydrophobic cores in apomyoglobin: A proton NMR spectroscopy study. Biochemistry, 29, 11067-11072 (1990).
    • (1990) Biochemistry , vol.29 , pp. 11067-11072
    • Cocco, M.J.1    Lecomte, J.T.J.2
  • 3
    • 0028466393 scopus 로고
    • Molten globular characteristics of the native state of apomyoglobin
    • L. Lin, R. J. Pinker, G. D. Rose, and N.R. Kallenbach: Molten globular characteristics of the native state of apomyoglobin. Struct. Biol., 1, 447-452 (1994).
    • (1994) Struct. Biol. , vol.1 , pp. 447-452
    • Lin, L.1    Pinker, R.J.2    Rose, G.D.3    Kallenbach, N.R.4
  • 4
    • 0028158780 scopus 로고
    • Solvent and thermal denaturation of the acidic compact state of apomyoglobin
    • I. Sirangelo, E. Bismuto, and G. Irace: Solvent and thermal denaturation of the acidic compact state of apomyoglobin. FEBS Lett., 338, 11-15 (1994).
    • (1994) FEBS Lett. , vol.338 , pp. 11-15
    • Sirangelo, I.1    Bismuto, E.2    Irace, G.3
  • 5
    • 0028329347 scopus 로고
    • Thermodynamic puzzle of apomyoglobin unfolding
    • Y. V. Griko and P. L. Privalov: Thermodynamic puzzle of apomyoglobin unfolding. J. Mol. Biol., 235, 1318-1325 (1994).
    • (1994) J. Mol. Biol. , vol.235 , pp. 1318-1325
    • Griko, Y.V.1    Privalov, P.L.2
  • 6
    • 0027245421 scopus 로고
    • Three-state analysis of sperm whale apomyoglobin folding
    • D. Barrick and R. L. Baldwin: Three-state analysis of sperm whale apomyoglobin folding. Biochemistry, 32, 3790-3796 (1993).
    • (1993) Biochemistry , vol.32 , pp. 3790-3796
    • Barrick, D.1    Baldwin, R.L.2
  • 7
    • 0028235775 scopus 로고
    • Molecular mechanisms of acid denaturation: The role of histidine residues in the partial unfolding of apomyoglobin
    • D. Barrick, F. M. Hughson, and R. L. Baldwin: Molecular mechanisms of acid denaturation: The role of histidine residues in the partial unfolding of apomyoglobin. J. Mol. Biol., 237, 588-601 (1994).
    • (1994) J. Mol. Biol. , vol.237 , pp. 588-601
    • Barrick, D.1    Hughson, F.M.2    Baldwin, R.L.3
  • 8
    • 0027933583 scopus 로고
    • Unfolding partway of apomyoglobin: Simultaneous characterization of acidic conformational states by frequency domain fluorometry
    • E. Bismuto and G. Irace: Unfolding partway of apomyoglobin: Simultaneous characterization of acidic conformational states by frequency domain fluorometry. J. Mol. Biol., 241, 103-109 (1994).
    • (1994) J. Mol. Biol. , vol.241 , pp. 103-109
    • Bismuto, E.1    Irace, G.2
  • 9
    • 0028361968 scopus 로고
    • Structural origins of pH and ionic strength effects on protein stability: Acid denaturation of sperm whale apomyoglobin
    • A.-S. Yang and B. Honig: Structural origins of pH and ionic strength effects on protein stability: Acid denaturation of sperm whale apomyoglobin. J. Mol. Biol., 237, 602-614 (1994).
    • (1994) J. Mol. Biol. , vol.237 , pp. 602-614
    • Yang, A.-S.1    Honig, B.2
  • 10
    • 0019883167 scopus 로고
    • Tryptophanyl fluorescence heterogeneity of apomyoglobins. Correlation with the presence of two distinct structural domains
    • G. Irace, C. Balestrieri, G. Parlato, L. Servillo, and G. Colonna: Tryptophanyl fluorescence heterogeneity of apomyoglobins. Correlation with the presence of two distinct structural domains. Biochemistry, 20, 792-799 (1981).
    • (1981) Biochemistry , vol.20 , pp. 792-799
    • Irace, G.1    Balestrieri, C.2    Parlato, G.3    Servillo, L.4    Colonna, G.5
  • 11
    • 0020486597 scopus 로고
    • Heme and cysteine microenvironments of tuna apomyoglobin. Evidence of two independent unfolding regions
    • G. Colonna, C. Balestrieri, E. Bismuto, L. Servillo, and G. Irace: Heme and cysteine microenvironments of tuna apomyoglobin. Evidence of two independent unfolding regions. Biochemistry, 21, 212-215 (1982).
    • (1982) Biochemistry , vol.21 , pp. 212-215
    • Colonna, G.1    Balestrieri, C.2    Bismuto, E.3    Servillo, L.4    Irace, G.5
  • 12
    • 0024294305 scopus 로고
    • Effect of unfolding on the tryptophanyl fluorescence lifetime distribution in apomyoglobin
    • E. Bismuto, E. Gratton, and G. Irace: Effect of unfolding on the tryptophanyl fluorescence lifetime distribution in apomyoglobin. Biochemistry, 27, 2132-2136 (1988).
    • (1988) Biochemistry , vol.27 , pp. 2132-2136
    • Bismuto, E.1    Gratton, E.2    Irace, G.3
  • 13
    • 0024464107 scopus 로고
    • Conformational substates of myoglobin detected by extrinsic dynamic fluorescence studies
    • E. Bismuto, I. Sirangelo, and G. Irace: Conformational substates of myoglobin detected by extrinsic dynamic fluorescence studies. Biochemistry, 28, 7542-7545 (1989).
    • (1989) Biochemistry , vol.28 , pp. 7542-7545
    • Bismuto, E.1    Sirangelo, I.2    Irace, G.3
  • 14
    • 0011762658 scopus 로고    scopus 로고
    • Studies on thermal denaturation of fish myoglobins using differential scanning calorimetry, circular dichroism, and tryptophan fluorescence
    • submitted
    • S. Chanthai, M. Ogawa, T. Tamiya, and T. Tsuchiya: Studies on thermal denaturation of fish myoglobins using differential scanning calorimetry, circular dichroism, and tryptophan fluorescence. Fisheries Sci., (submitted) (1996).
    • (1996) Fisheries Sci.
    • Chanthai, S.1    Ogawa, M.2    Tamiya, T.3    Tsuchiya, T.4
  • 15
    • 0014429123 scopus 로고
    • Comparison of myoglobins from harber seal, porpoise, and sperm whale. I. Preparation and characterization
    • K. D. Happer, R. A. Bradshaw, C. R. Hartzell, and F. R. N. Gurd: Comparison of myoglobins from harber seal, porpoise, and sperm whale. I. Preparation and characterization. J. Biol. Chem., 243, 683-689 (1968).
    • (1968) J. Biol. Chem. , vol.243 , pp. 683-689
    • Happer, K.D.1    Bradshaw, R.A.2    Hartzell, C.R.3    Gurd, F.R.N.4
  • 16
    • 0017112522 scopus 로고
    • Yellowfin tuna (Thunnus albacares) myoglobin: Characterization and comparative stability
    • G. J. Fosmiri and W. D. Brown: Yellowfin tuna (Thunnus albacares) myoglobin: Characterization and comparative stability. Comp. Biochem. Physiol., 55B, 293-299 (1976).
    • (1976) Comp. Biochem. Physiol. , vol.55 B , pp. 293-299
    • Fosmiri, G.J.1    Brown, W.D.2
  • 17
    • 0017831702 scopus 로고
    • Physical methods for the study of myoglobin
    • T. Rothgeb and F. R. N. Gurd: Physical methods for the study of myoglobin. In: Meth. in Enzymol., 52, 472-493 (1978).
    • (1978) Meth. in Enzymol. , vol.52 , pp. 472-493
    • Rothgeb, T.1    Gurd, F.R.N.2
  • 18
    • 0000707259 scopus 로고
    • Relative conformational changes of myoglobin and apomyoglobin
    • S. C. Harrison and E. R. Bluot: Relative conformational changes of myoglobin and apomyoglobin. J. Biol. Chem., 240, 299-303 (1965).
    • (1965) J. Biol. Chem. , vol.240 , pp. 299-303
    • Harrison, S.C.1    Bluot, E.R.2
  • 19
    • 77956741418 scopus 로고
    • Ultraviolet spectra of proteins and amino acids
    • D. B. Wetlaufer: Ultraviolet spectra of proteins and amino acids. Adv. Protein Chem., 17, 303-390 (1962).
    • (1962) Adv. Protein Chem. , vol.17 , pp. 303-390
    • Wetlaufer, D.B.1
  • 20
    • 0000085903 scopus 로고
    • Changes in side chain reactivity accompanying the binding of heme to sperm whale apomyoglobin
    • E. Breslow: Changes in side chain reactivity accompanying the binding of heme to sperm whale apomyoglobin. J. Biol. Chem., 239, 486-496 (1964).
    • (1964) J. Biol. Chem. , vol.239 , pp. 486-496
    • Breslow, E.1
  • 21
    • 11344291497 scopus 로고
    • The ultraviolet circular dichroism of polypeptides
    • G. Holzwarth and P. Doty: The ultraviolet circular dichroism of polypeptides. J. Am. Chem. Soc., 87, 218-228 (1965).
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 218-228
    • Holzwarth, G.1    Doty, P.2
  • 22
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: A fluorescent probe of non-polar binding sites
    • L. Stryer: The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: A fluorescent probe of non-polar binding sites. J. Mol. Biol., 13, 482-495 (1965).
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 23
    • 0020981508 scopus 로고
    • Structural and functional aspects of the heart ventricle myoglobin of bluefin tuna
    • G. Colonna, G. Irace, E. Bismuto, L. Servillo, and C. Balestrieri: Structural and functional aspects of the heart ventricle myoglobin of bluefin tuna. Comp. Biochem. Physiol., 76A, 481-485 (1983).
    • (1983) Comp. Biochem. Physiol. , vol.76 A , pp. 481-485
    • Colonna, G.1    Irace, G.2    Bismuto, E.3    Servillo, L.4    Balestrieri, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.