메뉴 건너뛰기




Volumn 12, Issue 3, 1999, Pages 219-225

Fluorescence and circular dichroism spectroscopic studies on bovine lactoperoxidase

Author keywords

Circular dichroism; Energy transfer; Fluorescence; Guanidine hydrochloride; Lactoperoxidase; Urea

Indexed keywords

ACRYLAMIDE; AMIDE; CESIUM ION; GUANIDINE; HEME; IODIDE ION; LACTOPEROXIDASE; LIGAND; TRYPTOPHAN; UREA;

EID: 0032886068     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1009207331434     Document Type: Article
Times cited : (9)

References (25)
  • 1
    • 0020479709 scopus 로고
    • Estimation of the free energy of stabilization of ribonulease A, lysozyme, α-lactoglobulin and myoglobin
    • Ahamad F, Bigelow C. 1982. Estimation of the free energy of stabilization of ribonulease A, lysozyme, α-lactoglobulin and myoglobin. J Biol Chem 257, 12935-12938.
    • (1982) J Biol Chem , vol.257 , pp. 12935-12938
    • Ahamad, F.1    Bigelow, C.2
  • 2
    • 0021115858 scopus 로고
    • Unfolding pathway of myoglobin. Evidence of multistate process
    • Bismuto E, Colonna G, Irace G. 1983 Unfolding pathway of myoglobin. Evidence of multistate process. Biochemistry 22, 4165-4170.
    • (1983) Biochemistry , vol.22 , pp. 4165-4170
    • Bismuto, E.1    Colonna, G.2    Irace, G.3
  • 3
    • 0025811540 scopus 로고
    • Primary structure of bovine lactoperoxidase, fourth member of a mammalian heme peroxidase family
    • Cals CM, Mailliart P, Brignon G, Anglade P, Dumas BR. 1991 Primary structure of bovine lactoperoxidase, fourth member of a mammalian heme peroxidase family. Eur J Biochem 198, 733-739.
    • (1991) Eur J Biochem , vol.198 , pp. 733-739
    • Cals, C.M.1    Mailliart, P.2    Brignon, G.3    Anglade, P.4    Dumas, B.R.5
  • 4
    • 0014462071 scopus 로고
    • Physical and compositional investigations of sub fractions of lactoperoxidase
    • Calstrom A. 1969 Physical and compositional investigations of sub fractions of lactoperoxidase, Acta Chem Scand 23, 171-213.
    • (1969) Acta Chem Scand , vol.23 , pp. 171-213
    • Calstrom, A.1
  • 6
    • 0021100329 scopus 로고
    • Identification, purification, and characterisation of a non-heme lactoperoxidase in bovine milk
    • Dumontet C, Rousset B. 1983 Identification, purification, and characterisation of a non-heme lactoperoxidase in bovine milk. J Biol Chem 258, 14166-14172.
    • (1983) J Biol Chem , vol.258 , pp. 14166-14172
    • Dumontet, C.1    Rousset, B.2
  • 7
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins, quantitative determination by fluorescence quenching studies
    • Eftink MR, Ghiron CA. 1976 Exposure of tryptophanyl residues in proteins, quantitative determination by fluorescence quenching studies. Biochemistry 15, 672-680.
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 9
    • 0027295704 scopus 로고
    • Quenching of intrinsic fluorescence of yeast cytochrome c peroxidase by covalently and non-covalently-bound quenchers
    • Fox T, Ferreira-rajabi L, Hill BC, English AN. 1993 Quenching of intrinsic fluorescence of yeast cytochrome c peroxidase by covalently and non-covalently-bound quenchers. Biochemistry 32, 6938-6943.
    • (1993) Biochemistry , vol.32 , pp. 6938-6943
    • Fox, T.1    Ferreira-Rajabi, L.2    Hill, B.C.3    English, A.N.4
  • 10
    • 3042995998 scopus 로고    scopus 로고
    • A theoretical three-dimensional model for lactoperoxidase and eosinophil peroxidase, built on the scafold of the myleoperoxidase x-ray structure
    • Gioia LD, Ghibaudi EM, Laurenti E, Salmona M, Ferrari RP. 1996 A theoretical three-dimensional model for lactoperoxidase and eosinophil peroxidase, built on the scafold of the myleoperoxidase x-ray structure. J Biol Inorg Chem 1, 476-488.
    • (1996) J Biol Inorg Chem , vol.1 , pp. 476-488
    • Gioia, L.D.1    Ghibaudi, E.M.2    Laurenti, E.3    Salmona, M.4    Ferrari, R.P.5
  • 11
    • 0016292941 scopus 로고
    • Urea, guanidine hydrochloride denuturation of ribonuclease, lysozyme α-cymotrypsin and β-lactoglobulin
    • Greene RF Jr. Pace CN. 1974 Urea, guanidine hydrochloride denuturation of ribonuclease, lysozyme α-cymotrypsin and β-lactoglobulin. J Biol Chem 249, 5388-5393.
    • (1974) J Biol Chem , vol.249 , pp. 5388-5393
    • Greene R.F., Jr.1    Pace, C.N.2
  • 12
    • 0018267881 scopus 로고
    • Effect of the orientation of donor and acceptor on the probably of electronic transitions of mixed polarisation
    • Haas E, Katchalski-Katzir E. 1978 Effect of the orientation of donor and acceptor on the probably of electronic transitions of mixed polarisation. Biochemistry 17, 5064-5070.
    • (1978) Biochemistry , vol.17 , pp. 5064-5070
    • Haas, E.1    Katchalski-Katzir, E.2
  • 13
    • 0022450503 scopus 로고
    • Detection, characterization, and quenching of the intrinsic fluorescence of bovine heart cytochrome c oxidase
    • Hill BC, Horowitz PM, Robinson NC. 1986 Detection, characterization, and quenching of the intrinsic fluorescence of bovine heart cytochrome c oxidase. Biochemistry 25, 2287-2292.
    • (1986) Biochemistry , vol.25 , pp. 2287-2292
    • Hill, B.C.1    Horowitz, P.M.2    Robinson, N.C.3
  • 14
    • 0023082770 scopus 로고
    • Chemical reduction of disulfides
    • Jocelyn PC. 1987 Chemical reduction of disulfides. Meth Enzymol 143, 246-249.
    • (1987) Meth Enzymol , vol.143 , pp. 246-249
    • Jocelyn, P.C.1
  • 16
    • 0021101610 scopus 로고
    • Rotational freedom of tryptophan residues in proteins and peptides
    • Lakowicz JR, Maliwal BP, Cherek H, Balter A. 1983 Rotational freedom of tryptophan residues in proteins and peptides. Biochemistry 22, 1741-1743.
    • (1983) Biochemistry , vol.22 , pp. 1741-1743
    • Lakowicz, J.R.1    Maliwal, B.P.2    Cherek, H.3    Balter, A.4
  • 17
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence, the quenching of tryptophenyl fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer SS. 1971 Solute perturbation of protein fluorescence, the quenching of tryptophenyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10, 3254-3263.
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 20
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. 1986 Determination and analysis of urea and guanidine hydrochloride denaturation curves. Meth Enzymol 131, 266-280.
    • (1986) Meth Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 21
    • 0027402748 scopus 로고
    • A step towards understanding the folding mechanism of horscradish peroxidase
    • Pappa HS, Cass AT. 1993 A step towards understanding the folding mechanism of horscradish peroxidase. Eur J Biochem 212, 227-235.
    • (1993) Eur J Biochem , vol.212 , pp. 227-235
    • Pappa, H.S.1    Cass, A.T.2
  • 22
    • 0002607532 scopus 로고
    • Biochemistry of peroxidase system: Antimicrobial effects
    • Pruitt KM. Reiter Tenovuo JO (ed) New York: Marcel Dekker
    • Pruitt KM, Reiter B. 1985 Biochemistry of peroxidase system: antimicrobial effects, in Pruitt KM. Reiter Tenovuo JO (ed) The Lactoperoxidase System. New York: Marcel Dekker; 143-177.
    • (1985) The Lactoperoxidase System , pp. 143-177
    • Pruitt, K.M.1    Reiter, B.2
  • 23
    • 0019331929 scopus 로고
    • Structure of milk lactoperoxidase: A study using circular dichroism and difference absorption spectroscopy
    • Sievers G. 1980 Structure of milk lactoperoxidase: A study using circular dichroism and difference absorption spectroscopy. Biochim Biophys Acta 624, 249-259.
    • (1980) Biochim Biophys Acta , vol.624 , pp. 249-259
    • Sievers, G.1
  • 24
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Snell EE, Boyer PD, Richardson C (eds)
    • Stryer L. 1978 Fluorescence energy transfer as a spectroscopic ruler. In: Snell EE, Boyer PD, Richardson C (eds) Ann Rev Biochem 47, 819-846.
    • (1978) Ann Rev Biochem , vol.47 , pp. 819-846
    • Stryer, L.1
  • 25
    • 0019882308 scopus 로고
    • The protoporphyrin-apoperoxidase complex as a horscradish peroxidase analog a fluorometric study of the heme pocket
    • Ugarova NN, Savitski AP, Berzein IV. 1981 The protoporphyrin-apoperoxidase complex as a horscradish peroxidase analog a fluorometric study of the heme pocket. Biochim Biophys Acta 662, 210-219.
    • (1981) Biochim Biophys Acta , vol.662 , pp. 210-219
    • Ugarova, N.N.1    Savitski, A.P.2    Berzein, I.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.