메뉴 건너뛰기




Volumn 46, Issue 7, 1998, Pages 2671-2677

Hydrophobicity of Bovine Serum Albumin and Ovalbumin Determined Using Uncharged (PRODAN) and Anionic (ANS-) Fluorescent Probes

Author keywords

ANS; Electrostatic interactions; Fluorescent probe; PRODAN; Protein hydrophobicity

Indexed keywords

BOVINAE;

EID: 0001296380     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf970876y     Document Type: Article
Times cited : (426)

References (35)
  • 1
    • 0014672131 scopus 로고
    • The effects that the environment exerts on the spectroscopic properties of certain dyes that are bound by bovine serum albumin
    • Ainsworth, S.; Flanagan, M. T. The effects that the environment exerts on the spectroscopic properties of certain dyes that are bound by bovine serum albumin. Biochim. Biophys. Acta 1969, 194, 213-221.
    • (1969) Biochim. Biophys. Acta , vol.194 , pp. 213-221
    • Ainsworth, S.1    Flanagan, M.T.2
  • 2
    • 0001506394 scopus 로고
    • Probing the binding site of bacterio-rhodopain with a fluorescent chromophore
    • Baasov, T.; Sheves, M. Probing the binding site of bacterio-rhodopain with a fluorescent chromophore. J. Am. Chem. Soc. 1987, 109, 1594-1596.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 1594-1596
    • Baasov, T.1    Sheves, M.2
  • 3
    • 0002670068 scopus 로고
    • Serum albumin: Structure and characterization of its ligand binding sites
    • Jost, P. C., Griffith, O. H., Eds.; Wiley-Interscience: New York
    • Brown, J. R.; Shockley, P. Serum albumin: Structure and characterization of its ligand binding sites. In Lipid - Protein Interactions; Jost, P. C., Griffith, O. H., Eds.; Wiley-Interscience: New York, 1982; Vol. 1, pp 25-68.
    • (1982) Lipid - Protein Interactions , vol.1 , pp. 25-68
    • Brown, J.R.1    Shockley, P.2
  • 4
    • 0029417213 scopus 로고
    • Substrate-induced translocation of PKC-α to the membrane
    • Bruins, R. H.; Epand, R. M. Substrate-induced translocation of PKC-α to the membrane. Arch. Biochem. Biophys. 1995, 324, 216-222.
    • (1995) Arch. Biochem. Biophys. , vol.324 , pp. 216-222
    • Bruins, R.H.1    Epand, R.M.2
  • 5
    • 84989695101 scopus 로고
    • A photophysical study of solvatochromic probe 6-propionyl-2-(N,N-dimethylamino)-naphthalene (Prodan) in solution
    • Bunker, C. E.; Bowen, T. L.; Sun, Y.-P. A photophysical study of solvatochromic probe 6-propionyl-2-(N,N-dimethylamino)-naphthalene (Prodan) in solution. Photochem. Photobiol. 1993, 58, 499-505.
    • (1993) Photochem. Photobiol. , vol.58 , pp. 499-505
    • Bunker, C.E.1    Bowen, T.L.2    Sun, Y.-P.3
  • 6
    • 0026514355 scopus 로고
    • Spectrofluorimetric assessment of the surface hydrophobicity of proteins
    • Cardamone, M.; Puri, N. K. Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochem. J. 1992, 282, 589-593.
    • (1992) Biochem. J. , vol.282 , pp. 589-593
    • Cardamone, M.1    Puri, N.K.2
  • 7
    • 0030582316 scopus 로고    scopus 로고
    • Fluorescence of spectrin-bound Prodan
    • Chakrabarti, A. Fluorescence of spectrin-bound Prodan. Biochem. Biophys. Res. Commun. 1996, 226, 495-497.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 495-497
    • Chakrabarti, A.1
  • 8
    • 0013913906 scopus 로고
    • Cooperative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalene-sulfonate. Fluorimetric Titrations
    • Daniel, E.; Weber, G. Cooperative effects in binding by bovine serum albumin. I. The binding of 1-anilino-8-naphthalene-sulfonate. Fluorimetric Titrations. Biochemistry 1966, 5, 1893-1900.
    • (1966) Biochemistry , vol.5 , pp. 1893-1900
    • Daniel, E.1    Weber, G.2
  • 10
    • 4043065847 scopus 로고
    • The apomyoglobin-arylaminonaphthalenesulfonate system. Insight into fluorescent probe responses by substituent modulation
    • Dodiuk, H.; Kanety, H.; Kosower, E. M. The apomyoglobin-arylaminonaphthalenesulfonate system. Insight into fluorescent probe responses by substituent modulation. J. Phys. Chem. 1979, 83, 515-521.
    • (1979) J. Phys. Chem. , vol.83 , pp. 515-521
    • Dodiuk, H.1    Kanety, H.2    Kosower, E.M.3
  • 11
    • 0022365532 scopus 로고
    • Circular dichroic and fluorometric studies on the acid-induced isomerization of bovine plasma albumin- 1-anilino-8-naphthale-nesulfonate complex
    • Era, S.; Kuwata, K.; Kida, K.; Sogami, M.; Yoshida, A. Circular dichroic and fluorometric studies on the acid-induced isomerization of bovine plasma albumin-1-anilino-8-naphthale-nesulfonate complex. Int. J. Pept. Protein Res. 1986, 26, 575-583.
    • (1986) Int. J. Pept. Protein Res. , vol.26 , pp. 575-583
    • Era, S.1    Kuwata, K.2    Kida, K.3    Sogami, M.4    Yoshida, A.5
  • 13
    • 0000629760 scopus 로고
    • The denaturation of proteins. II. Ultraviolet absorption spectra of bovine serum albumin and ovalbumin in urea and in acid solution
    • Glazer, A. N.; McKenzie, H. A.; Wake, R. G. The denaturation of proteins. II. Ultraviolet absorption spectra of bovine serum albumin and ovalbumin in urea and in acid solution. Biochim. Biophys. Acta 1963, 69, 240-248.
    • (1963) Biochim. Biophys. Acta , vol.69 , pp. 240-248
    • Glazer, A.N.1    McKenzie, H.A.2    Wake, R.G.3
  • 14
    • 0342578388 scopus 로고
    • Interactions of anionic and cationic fluorescent probes with proteins: The effect of charge
    • Greene, F. C. Interactions of anionic and cationic fluorescent probes with proteins: The effect of charge. J. Protein Chem. 1984, 3, 167-179.
    • (1984) J. Protein Chem. , vol.3 , pp. 167-179
    • Greene, F.C.1
  • 15
    • 0001293843 scopus 로고    scopus 로고
    • Cooperative binding of 6-(p-toluidinyl)naphthalene-2-sulfonate by β-cyclodextrin dimers
    • Haskard, C. A.; Easton, C. J.; May, B. L.; Lincoln, S. F. Cooperative binding of 6-(p-toluidinyl)naphthalene-2-sulfonate by β-cyclodextrin dimers. J. Phys. Chem. 1996, 100, 14457-14461.
    • (1996) J. Phys. Chem. , vol.100 , pp. 14457-14461
    • Haskard, C.A.1    Easton, C.J.2    May, B.L.3    Lincoln, S.F.4
  • 16
    • 84985200365 scopus 로고
    • Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins
    • Hayakawa, S.; Nakai, S. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. J. Food Sci. 1985, 50, 486-491.
    • (1985) J. Food Sci. , vol.50 , pp. 486-491
    • Hayakawa, S.1    Nakai, S.2
  • 17
    • 0015221771 scopus 로고
    • Presence of arginine residues at the strong hydrophobic anion binding sites of bovine serum albumin
    • Jonas, A.; Weber, G. Presence of arginine residues at the strong hydrophobic anion binding sites of bovine serum albumin. Biochemistry 1971, 10, 1335-1339.
    • (1971) Biochemistry , vol.10 , pp. 1335-1339
    • Jonas, A.1    Weber, G.2
  • 18
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • Kato, A.; Nakai, S. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim. Biophys. Acta 1980, 624, 13-20.
    • (1980) Biochim. Biophys. Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 19
    • 0030023342 scopus 로고    scopus 로고
    • Spectral properties of environmentally sensitive probes associated with horseradish peroxidase
    • Lasagna, M.; Vargas, V.; Jameson, D. M.; Brunet, J. E. Spectral properties of environmentally sensitive probes associated with horseradish peroxidase. Biochemistry 1996, 36, 973-979.
    • (1996) Biochemistry , vol.36 , pp. 973-979
    • Lasagna, M.1    Vargas, V.2    Jameson, D.M.3    Brunet, J.E.4
  • 20
    • 0041795454 scopus 로고
    • Hydrophobicity in food protein systems
    • Hui, Y. H., Ed.; Wiley: New York
    • Li-Chan, E. Hydrophobicity in food protein systems. In Encyclopedia of Food Science and Technology; Hui, Y. H., Ed.; Wiley: New York, 1991; pp 1429-1439.
    • (1991) Encyclopedia of Food Science and Technology , pp. 1429-1439
    • Li-Chan, E.1
  • 21
    • 0022643095 scopus 로고
    • Estimation of the polarity of the protein interior by optical spectroscopy
    • MacGregor, R. B.; Weber, G. Estimation of the polarity of the protein interior by optical spectroscopy. Nature 1986, 319, 70-73.
    • (1986) Nature , vol.319 , pp. 70-73
    • MacGregor, R.B.1    Weber, G.2
  • 23
    • 0002962718 scopus 로고    scopus 로고
    • Measurement of surface hydrophobicity
    • Hall, G. M., Ed.; Blackie Academic & Professional, An Imprint of Chapman & Hall: London, U.K.
    • Nakai, S.; Li-Chan, E.; Arteaga, G. E. Measurement of surface hydrophobicity. In Methods of Testing Protein Functionality; Hall, G. M., Ed.; Blackie Academic & Professional, An Imprint of Chapman & Hall: London, U.K., 1996; pp 226-259.
    • (1996) Methods of Testing Protein Functionality , pp. 226-259
    • Nakai, S.1    Li-Chan, E.2    Arteaga, G.E.3
  • 25
    • 0028793377 scopus 로고
    • Effects of ionic strength and pH on the binding of medium-chain fatty acids to human serum albumin
    • Pederson, A. O.; Mensberg, K.-L. D.; Kragh-Hansen, U. Effects of ionic strength and pH on the binding of medium-chain fatty acids to human serum albumin. Eur. J. Biochem. 1995, 233, 395-405.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 395-405
    • Pederson, A.O.1    Mensberg, K.-L.D.2    Kragh-Hansen, U.3
  • 26
    • 0015507609 scopus 로고
    • 1-Anilinonaphthalene-8-sulfonate. The dependence of emission spectra on molecular formation studied by fluorescence and proton magnetic resonance
    • Penzer, G. 1-Anilinonaphthalene-8-sulfonate. The dependence of emission spectra on molecular formation studied by fluorescence and proton magnetic resonance. Eur. J. Biochem. 1972, 25, 218-228.
    • (1972) Eur. J. Biochem. , vol.25 , pp. 218-228
    • Penzer, G.1
  • 27
    • 0000164429 scopus 로고
    • A comparison of optimization methods for fitting curves to infrared band envelopes
    • Pitha, J.; Jones, R. N. A comparison of optimization methods for fitting curves to infrared band envelopes. Can. J. Chem. 1966, 44, 3031-3050.
    • (1966) Can. J. Chem. , vol.44 , pp. 3031-3050
    • Pitha, J.1    Jones, R.N.2
  • 29
    • 0026787836 scopus 로고
    • Probing the interactions of alcohols with biological membranes with the fluorescent probe Prodan
    • Rottenberg, H. Probing the interactions of alcohols with biological membranes with the fluorescent probe Prodan. Biochemistry 1992, 31, 9473-9481.
    • (1992) Biochemistry , vol.31 , pp. 9473-9481
    • Rottenberg, H.1
  • 31
    • 0025949027 scopus 로고
    • Crystal structured of uncleaved ovalbumin at 1.95 a resolution
    • Stein, P. E.; Leslie, A. G. W.; Finch, J. T.; Carrell, R. W. Crystal structured of uncleaved ovalbumin at 1.95 A resolution. J. Mol. Biol. 1991, 221, 941-959.
    • (1991) J. Mol. Biol. , vol.221 , pp. 941-959
    • Stein, P.E.1    Leslie, A.G.W.2    Finch, J.T.3    Carrell, R.W.4
  • 32
    • 0042486775 scopus 로고
    • A simple fluorometric method for fat-binding capacity as an index of hydrophobicity of proteins
    • Tsutsui, T.; Li-Chan, E.; Nakai, S. A simple fluorometric method for fat-binding capacity as an index of hydrophobicity of proteins. J. Food Sci. 1986, 51, 1268-1272.
    • (1986) J. Food Sci. , vol.51 , pp. 1268-1272
    • Tsutsui, T.1    Li-Chan, E.2    Nakai, S.3
  • 33
    • 0018786922 scopus 로고
    • Farris, F. J. Synthesis and spectral properties of a hydrophobic fluorescent probe: 6-Propionyl-2-(dimethylamino)naphthalene
    • Weber, G.; Farris, F. J. Synthesis and spectral properties of a hydrophobic fluorescent probe: 6-Propionyl-2-(dimethylamino)naphthalene. Biochemistry 1979, 18, 3075-3078.
    • (1979) Biochemistry , vol.18 , pp. 3075-3078
    • Weber, G.1
  • 34
    • 78651030061 scopus 로고
    • Fluorescent indicators of adsorption in aqueous solution and on the solid phase
    • Weber, G.; Laurence, D. J. R. Fluorescent indicators of adsorption in aqueous solution and on the solid phase. Biochem. J. 1954, 56, xxxi.
    • (1954) Biochem. J. , vol.56
    • Weber, G.1    Laurence, D.J.R.2
  • 35
    • 0000478993 scopus 로고
    • Fragmentation of bovine serum albumin by pepsin. I. The origin of the acid expansion of the albumin molecule
    • Weber, G.; Young, L. B. Fragmentation of bovine serum albumin by pepsin. I. The origin of the acid expansion of the albumin molecule. J. Biol. Chem. 1964, 239, 1415-1423.
    • (1964) J. Biol. Chem. , vol.239 , pp. 1415-1423
    • Weber, G.1    Young, L.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.