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Volumn 18, Issue 1, 2008, Pages 11-15

Study on the interaction mechanism of lysozyme and bromophenol blue by fluorescence spectroscopy

Author keywords

Bromophenol blue; Fluorescence quenching; Lysozyme

Indexed keywords

BROMOPHENOL BLUE; FLUORESCENCE QUENCHING; LYSOZYME;

EID: 38149063469     PISSN: 10530509     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10895-007-0228-7     Document Type: Article
Times cited : (25)

References (27)
  • 1
    • 1842776297 scopus 로고
    • Shandong Science and Technology Press Beijing
    • Sheng CJ, Dian HD (1982) Lysozyme. Shandong Science and Technology Press, Beijing, pp 50-51
    • (1982) Lysozyme , pp. 50-51
    • Sheng, C.J.1    Dian, H.D.2
  • 2
    • 0037355647 scopus 로고    scopus 로고
    • A new analytical procedure for assay of lysozyme in human tear and saliva with immobilized reagents in flow injection chemiluminescence system
    • Song ZH, Hou S (2003) A new analytical procedure for assay of lysozyme in human tear and saliva with immobilized reagents in flow injection chemiluminescence system. Anal Sci 19:347-352
    • (2003) Anal Sci , vol.19 , pp. 347-352
    • Song, Z.H.1    Hou, S.2
  • 3
    • 0023792625 scopus 로고
    • Interactions between cations in modifying the binding of hexokinases i and II to mitochondria
    • Imai N, Akimoto H, Oda M, Okazaki M, Ishibashi S, Kurokawa M (1988) Interactions between cations in modifying the binding of hexokinases I and II to mitochondria. Mol Cell Biochem 81:37-41
    • (1988) Mol Cell Biochem , vol.81 , pp. 37-41
    • Imai, N.1    Akimoto, H.2    Oda, M.3    Okazaki, M.4    Ishibashi, S.5    Kurokawa, M.6
  • 4
    • 0037085669 scopus 로고    scopus 로고
    • FT-IR observation of covalent labelling of lysozyme crystals by organometallic complexes of transition metals
    • Egan D, Salmain M, McArdle P, Jaouen G, Caro B (2002) FT-IR observation of covalent labelling of lysozyme crystals by organometallic complexes of transition metals. Spectrochim Acta Part A Mol Biomol Spectrosc 58:941-951
    • (2002) Spectrochim Acta Part A Mol Biomol Spectrosc , vol.58 , pp. 941-951
    • Egan, D.1    Salmain, M.2    McArdle, P.3    Jaouen, G.4    Caro, B.5
  • 5
    • 2342511008 scopus 로고    scopus 로고
    • Lysozyme enhanced europium-metacycline complex fluorescence: A new spectrofluorimetric method for the determination of lysozyme
    • Jiang CQ, Luo L (2004) Lysozyme enhanced europium-metacycline complex fluorescence: a new spectrofluorimetric method for the determination of lysozyme. Anal Chim Acta 511:11-16
    • (2004) Anal Chim Acta , vol.511 , pp. 11-16
    • Jiang, C.Q.1    Luo, L.2
  • 6
    • 5144230465 scopus 로고    scopus 로고
    • 2+ binds to active site of hen egg-white lysozyme and quenches fluorescence of Trp62 and Trp108
    • 2+ binds to active site of hen egg-white lysozyme and quenches fluorescence of Trp62 and Trp108. Biochem Biophys Res Commun 324:529-533
    • (2004) Biochem Biophys Res Commun , vol.324 , pp. 529-533
    • Li, S.J.1    Nakagawa, A.2    Tsukihara, T.3
  • 7
    • 9644265496 scopus 로고    scopus 로고
    • Purification of lysozyme from egg white by Reactive Blue 4 and Reactive Red 120 dye-ligands immobilised composite membranes
    • ArIca MY, Bayramoǧlu G (2005) Purification of lysozyme from egg white by Reactive Blue 4 and Reactive Red 120 dye-ligands immobilised composite membranes. Process Biochem 40:1433-1442
    • (2005) Process Biochem , vol.40 , pp. 1433-1442
    • Arca, M.Y.1    Bayramolu, G.2
  • 8
    • 34548188047 scopus 로고    scopus 로고
    • Photochemical behavior of lysozyme-4-(2-pyridylazo)-resorcinol polymolecular complex and its analytical applications
    • DOI 10.1007/s10895-007-0202-4
    • Yue QL, Song ZH, Dong FX, Liu YH, Shao XD (2007) Photochemical behavior of lysozyme-4-(2-pyridylazo)-resorcinol polymolecular complex and its analytical applications. J Fluoresc DOI 10.1007/s10895-007-0202-4
    • (2007) J Fluoresc
    • Yue, Q.L.1    Zh, S.2    Dong, F.X.3    Liu, Y.H.4    Shao, X.D.5
  • 9
    • 0033924312 scopus 로고    scopus 로고
    • Lysozyme photo-oxidation by singlet oxygen: Properties of the partially inactivated enzyme
    • Silva E, Landea CD, Edwards AM, Lissi E (2000) Lysozyme photo-oxidation by singlet oxygen: properties of the partially inactivated enzyme. J Photochem Photobiol B Biol 55:196-200
    • (2000) J Photochem Photobiol B Biol , vol.55 , pp. 196-200
    • Silva, E.1    Landea, C.D.2    Edwards, A.M.3    Lissi, E.4
  • 10
    • 1842686905 scopus 로고    scopus 로고
    • Study of the interactions between tetracycline analogues and lysozyme
    • Jiang CQ, Wang T (2004) Study of the interactions between tetracycline analogues and lysozyme. Bioorg Med Chem 12:2043-2047
    • (2004) Bioorg Med Chem , vol.12 , pp. 2043-2047
    • Jiang, C.Q.1    Wang, T.2
  • 11
    • 0020476474 scopus 로고
    • Binding site of the dye in bromophenol blue-lysozyme complex proton magnetic resonance study in aqueous solutions
    • Krishnamoorthy G, Prabhananda BS (1982) Binding site of the dye in bromophenol blue-lysozyme complex proton magnetic resonance study in aqueous solutions. Biochim Biophys Acta 709:53-57
    • (1982) Biochim Biophys Acta , vol.709 , pp. 53-57
    • Krishnamoorthy, G.1    Prabhananda, B.S.2
  • 12
    • 0020488019 scopus 로고
    • Phenolsulfophthalein dyes as probes in the study of lysozyme activity towards cell wall substrates
    • Krishnamoorthy G, Prabhananda BS (1982) Phenolsulfophthalein dyes as probes in the study of lysozyme activity towards cell wall substrates. Biochim Biophys Acta 709:234-246
    • (1982) Biochim Biophys Acta , vol.709 , pp. 234-246
    • Krishnamoorthy, G.1    Prabhananda, B.S.2
  • 13
    • 0026633672 scopus 로고
    • Additional binding sites in lysozyme. X-ray analysis of lysozyme complexes with bromophenol red and bromophenol blue
    • Madhusudan VM (1992) Additional binding sites in lysozyme. X-ray analysis of lysozyme complexes with bromophenol red and bromophenol blue. Protein Eng 5:399-404
    • (1992) Protein Eng , vol.5 , pp. 399-404
    • Madhusudan, V.M.1
  • 14
    • 0021454769 scopus 로고
    • Interaction of lysozyme with dyes. II. Binding of bromophenol blue
    • Subramanian M, Heshadri BS, Venkatappa MP (1984) Interaction of lysozyme with dyes. II. Binding of bromophenol blue. J Biochem 96:245-252
    • (1984) J Biochem , vol.96 , pp. 245-252
    • Subramanian, M.1    Heshadri, B.S.2    Venkatappa, M.P.3
  • 15
    • 0015343130 scopus 로고
    • Fluorescence of lysozyme: Emissions from tryptophan residues 62 and 108 and energy migration
    • Imoto T, Forster LS, Rupley JA, Tanaka F (1971) Fluorescence of lysozyme: emissions from tryptophan residues 62 and 108 and energy migration. Proc Natl Acad Sci USA 69:1151-1155
    • (1971) Proc Natl Acad Sci USA , vol.69 , pp. 1151-1155
    • Imoto, T.1    Forster, L.S.2    Rupley, J.A.3    Tanaka, F.4
  • 17
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules
    • Lakowicz JR, Weber G (1973) Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules. Biochemistry 12:4161-4170
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • Lakowicz, J.R.1    Weber, G.2
  • 18
    • 1842426864 scopus 로고
    • Oxygen quenching of fluorescence in solution: An experimental study of the diffusion process
    • Ware WR (1962) Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process. J Phys Chem 66:455-458
    • (1962) J Phys Chem , vol.66 , pp. 455-458
    • Ware, W.R.1
  • 19
    • 0032495131 scopus 로고    scopus 로고
    • Investigation of the interaction between acridine orange and bovine serum albumin
    • Feng XZ, Lin Z, Yang LJ, Wang C, Bai CL (1998) Investigation of the interaction between acridine orange and bovine serum albumin. Talanta 47:1223-1229
    • (1998) Talanta , vol.47 , pp. 1223-1229
    • Feng, X.Z.1    Lin, Z.2    Yang, L.J.3    Wang, C.4    Bai, C.L.5
  • 20
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • Ross PD, Subramanian S (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20:3096-3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 22
    • 0017661379 scopus 로고
    • Conjugated polyene fatty acids as fluorescent probes: Binding to bovine serum albumin
    • Sklar LA, Hudson BS, Simoni RD (1977) Conjugated polyene fatty acids as fluorescent probes: binding to bovine serum albumin. Biochem 16:5100-5108
    • (1977) Biochem , vol.16 , pp. 5100-5108
    • Sklar, L.A.1    Hudson, B.S.2    Simoni, R.D.3
  • 27
    • 13444292204 scopus 로고    scopus 로고
    • Effect of Chinese medicine alpinetin on the structure of human serum albumin
    • He W, Li Y, Xue C, Hu Z, Chen X, Sheng F (2005) Effect of Chinese medicine alpinetin on the structure of human serum albumin. Bioorg Med Chem 13:1837-1845
    • (2005) Bioorg Med Chem , vol.13 , pp. 1837-1845
    • He, W.1    Li, Y.2    Xue, C.3    Hu, Z.4    Chen, X.5    Sheng, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.