메뉴 건너뛰기




Volumn 72, Issue 3, 2000, Pages 415-420

Fluorescence properties of pyrylretinol

Author keywords

[No Author keywords available]

Indexed keywords

3 METHYL 5 (1 PYRYL)PENTADIEN 1 OL; 3,7 DIMETHYL 9 (1 PYRYL)NONATETRAEN 1 OL; ALKENE DERIVATIVE; CHOLINE DERIVATIVE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; LIPOSOME; ORGANIC SOLVENT; PYRYLRETINOL; RETINOID BINDING PROTEIN; RETINOL DERIVATIVE; SERUM ALBUMIN; UNCLASSIFIED DRUG;

EID: 0034286854     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2000)072<0415:FPOP>2.0.CO;2     Document Type: Article
Times cited : (3)

References (31)
  • 1
    • 0025303725 scopus 로고
    • Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin
    • Birge, R. R. (1990) Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin. Biochim. Biophys. Acta 1016, 293-327.
    • (1990) Biochim. Biophys. Acta , vol.1016 , pp. 293-327
    • Birge, R.R.1
  • 2
    • 0002296721 scopus 로고
    • Plasma retinol-binding protein
    • Edited by M. B. Sporn, A. B. Roberts and D. S. Goodman. Raven Press, New York
    • Soprano, R. D. and W. S. Blaner (1994) Plasma retinol-binding protein. In The Retinoids - Biology, Chemistry and Medicine (Edited by M. B. Sporn, A. B. Roberts and D. S. Goodman), pp. 257-281. Raven Press, New York.
    • (1994) The Retinoids - Biology, Chemistry and Medicine , pp. 257-281
    • Soprano, R.D.1    Blaner, W.S.2
  • 3
    • 0003035905 scopus 로고
    • Cellular retinoid-binding proteins
    • Edited by M. B. Sporn, A. B. Roberts and D. S. Goodman. Raven Press, New York
    • Ong, D. E., M. E. Newcomer and F. Chytil (1994) Cellular retinoid-binding proteins. In The Retinoids - Biology, Chemistry and Medicine (Edited by M. B. Sporn, A. B. Roberts and D. S. Goodman), pp. 283-317. Raven Press, New York.
    • (1994) The Retinoids - Biology, Chemistry and Medicine , pp. 283-317
    • Ong, D.E.1    Newcomer, M.E.2    Chytil, F.3
  • 4
    • 85005558631 scopus 로고
    • Application of artificial pigments to structure determination and study of photoinduced transformations of retinal proteins
    • Nakanishi, K. and R. Crouch (1995) Application of artificial pigments to structure determination and study of photoinduced transformations of retinal proteins. Israel J. Chem. 35, 253-272.
    • (1995) Israel J. Chem. , vol.35 , pp. 253-272
    • Nakanishi, K.1    Crouch, R.2
  • 5
    • 0021869659 scopus 로고
    • 1-Palmitoyl-2-pyrenedecanoyl Glycerophospholipid as membrane probes: Evidence for regular distribution in liquid-crystalline phosphatidylcholine bilayers
    • Somerjaju, P. J., J. A. Virtanen, K. K. Eklund, P. Vainio, P. K. J. Kinnunen (1985) 1-Palmitoyl-2-pyrenedecanoyl Glycerophospholipid as membrane probes: evidence for regular distribution in liquid-crystalline phosphatidylcholine bilayers. Biochemistry 24, 2773-2781.
    • (1985) Biochemistry , vol.24 , pp. 2773-2781
    • Somerjaju, P.J.1    Virtanen, J.A.2    Eklund, K.K.3    Vainio, P.4    Kinnunen, P.K.J.5
  • 6
    • 0021830008 scopus 로고
    • Oxygen quenching of pyrene-lipid fluorescence in phosphatidylcholine vesicles - A probe for membrane organization
    • Chong, P. L.-G and T. E. Thompson (1985) Oxygen quenching of pyrene-lipid fluorescence in phosphatidylcholine vesicles - a probe for membrane organization. Biophys. J. 47, 613-621.
    • (1985) Biophys. J. , vol.47 , pp. 613-621
    • Chong, P.L.-G.1    Thompson, T.E.2
  • 7
    • 0024409236 scopus 로고
    • Pyrene-labeled lipids: Versatile probes of membrane dynamics in vitro and in living cells
    • Pownall, H. J. and L. C. Smith (1989) Pyrene-labeled lipids: versatile probes of membrane dynamics in vitro and in living cells. Chem. Phys. Lipids 50, 191-211.
    • (1989) Chem. Phys. Lipids , vol.50 , pp. 191-211
    • Pownall, H.J.1    Smith, L.C.2
  • 8
    • 0032546092 scopus 로고    scopus 로고
    • Synthesis of a chiral phospholipase-C and D insensitive membrane probe with excimer emission properties
    • Huang, G. and R. I. Hollingworth (1998) Synthesis of a chiral phospholipase-C and D insensitive membrane probe with excimer emission properties. Tetrahedron 54, 1355-1360.
    • (1998) Tetrahedron , vol.54 , pp. 1355-1360
    • Huang, G.1    Hollingworth, R.I.2
  • 9
    • 0026757117 scopus 로고
    • E/M dips. Evidence for lipids regularly distributed into hexagonal super-lattices in pyrene-PC/DMPC binary mixtures at specific concentrations
    • Tang, D. and P. L.-G. Chong (1992) E/M dips. Evidence for lipids regularly distributed into hexagonal super-lattices in pyrene-PC/DMPC binary mixtures at specific concentrations. Biophys. J. 63, 903-910.
    • (1992) Biophys. J. , vol.63 , pp. 903-910
    • Tang, D.1    Chong, P.L.-G.2
  • 10
    • 70449246528 scopus 로고
    • Phosphorous assay in column chromatography
    • Bartlett, G. R. (1959) Phosphorous assay in column chromatography, J. Biol. Chem. 234, 466-468.
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 12
    • 0019615405 scopus 로고
    • Correction of timing errors in photomultiplier tubes used in phase-modulation fluorometry
    • Lakowicz, J. R., H. Cherek and A. Balter (1981) Correction of timing errors in photomultiplier tubes used in phase-modulation fluorometry. J. Biochem. Biophys. Methods 5, 131-146.
    • (1981) J. Biochem. Biophys. Methods , vol.5 , pp. 131-146
    • Lakowicz, J.R.1    Cherek, H.2    Balter, A.3
  • 13
    • 0001420298 scopus 로고
    • Fluorescence enhancement of benzene derivatives by forming inclusion complexes with β-cyclodextrin in aqueous solutions
    • Hoshino, M., M. Imamura, K. Ikehara and Y. Hama (1981) Fluorescence enhancement of benzene derivatives by forming inclusion complexes with β-cyclodextrin in aqueous solutions. J. Phys. Chem. 85, 1820-1823.
    • (1981) J. Phys. Chem. , vol.85 , pp. 1820-1823
    • Hoshino, M.1    Imamura, M.2    Ikehara, K.3    Hama, Y.4
  • 14
    • 0032514240 scopus 로고    scopus 로고
    • Liposome-encapsulated vitamin A compounds show greater stability and diminished toxicity
    • Singh, A. K. and J. Das (1998) Liposome-encapsulated vitamin A compounds show greater stability and diminished toxicity. Biophys. Chem. 73, 155-162.
    • (1998) Biophys. Chem. , vol.73 , pp. 155-162
    • Singh, A.K.1    Das, J.2
  • 16
    • 2142760512 scopus 로고
    • Environmental effects on vibronic band intensities in pyrene monomer fluorescence and their application
    • Kalyansundaram, K. and J. K. Thomas (1977) Environmental effects on vibronic band intensities in pyrene monomer fluorescence and their application. J. Am. Chem. Soc. 99, 2039-2044.
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 2039-2044
    • Kalyansundaram, K.1    Thomas, J.K.2
  • 17
    • 0023277161 scopus 로고
    • A fluorescence study of dehydroergosterol in phosphatidylcholine bilayer vesicles
    • Schroeder, F., Y. Barenholz, E. Gratton and T. E. Thompson (1987) A fluorescence study of dehydroergosterol in phosphatidylcholine bilayer vesicles. Biochemistry 26, 2441-2448.
    • (1987) Biochemistry , vol.26 , pp. 2441-2448
    • Schroeder, F.1    Barenholz, Y.2    Gratton, E.3    Thompson, T.E.4
  • 18
    • 0013173905 scopus 로고
    • Retinol: A fluorescent probe for membrane lipids
    • Radda, G. K. and D. S. Smith (1970) Retinol: a fluorescent probe for membrane lipids. FEBS Lett. 9, 287-289.
    • (1970) FEBS Lett. , vol.9 , pp. 287-289
    • Radda, G.K.1    Smith, D.S.2
  • 19
    • 0016215159 scopus 로고
    • Pyrene. A probe of lateral diffusion in the hydrophobic region of membrane
    • Vanderkooi, J. M. and J. B. Callis (1974) Pyrene. A probe of lateral diffusion in the hydrophobic region of membrane. Biochemistry 13, 400-4006.
    • (1974) Biochemistry , vol.13 , pp. 400-4006
    • Vanderkooi, J.M.1    Callis, J.B.2
  • 20
    • 0016782319 scopus 로고
    • Oxygen diffusion in biological and artificial membranes determined by the fluorochrome pyrene
    • Fischkoff, S. and J. M. Vanderkooi (1975) Oxygen diffusion in biological and artificial membranes determined by the fluorochrome pyrene. J. Gen. Physiol. 65, 663-676.
    • (1975) J. Gen. Physiol. , vol.65 , pp. 663-676
    • Fischkoff, S.1    Vanderkooi, J.M.2
  • 21
    • 0032740652 scopus 로고    scopus 로고
    • Calorimetric and molecular mechanics studies of the thermotropic phase behavior of membrane phospholipids
    • Huang, C. and S. Li (1999) Calorimetric and molecular mechanics studies of the thermotropic phase behavior of membrane phospholipids. Biochim. Biophys. Acta 1422, 273-307.
    • (1999) Biochim. Biophys. Acta , vol.1422 , pp. 273-307
    • Huang, C.1    Li, S.2
  • 22
    • 0015523573 scopus 로고
    • The enhancement of fluorescence and the decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, β-lactoglobulin and the retinol-binding protein of human plasma
    • Futterman, S. and J. Heller (1972) The enhancement of fluorescence and the decreased susceptibility to enzymatic oxidation of retinol complexed with bovine serum albumin, β-lactoglobulin and the retinol-binding protein of human plasma. J. Biol. Chem. 247, 5168-5172.
    • (1972) J. Biol. Chem. , vol.247 , pp. 5168-5172
    • Futterman, S.1    Heller, J.2
  • 23
    • 0026901040 scopus 로고
    • Interphotoreceptor retinoid-binding protein and α-tocopherol preserve the isomeric and oxidation state of retinol
    • Crouch, R. K., E. S. Hazard, T. Lind, B. Wiggert, G. Chader and D. W. Corson (1992) Interphotoreceptor retinoid-binding protein and α-tocopherol preserve the isomeric and oxidation state of retinol. Photochem. Photobiol. 56, 251-255.
    • (1992) Photochem. Photobiol. , vol.56 , pp. 251-255
    • Crouch, R.K.1    Hazard, E.S.2    Lind, T.3    Wiggert, B.4    Chader, G.5    Corson, D.W.6
  • 24
    • 0030789433 scopus 로고    scopus 로고
    • Binding of the volatile anesthetic chloroform to albumin demonstrated using tryptophan fluorescence quenching
    • Johansson, J. S. (1997) Binding of the volatile anesthetic chloroform to albumin demonstrated using tryptophan fluorescence quenching. J. Biol. Chem. 272, 17961-17965.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17961-17965
    • Johansson, J.S.1
  • 25
    • 0028825488 scopus 로고
    • All-trans-N-retinylide-netryptamine Schiff base in surfactant solubilized water pools in heptane - A fluorescence study
    • Singh, A. K. and N. Majumdar (1995) All-trans-N-retinylide-netryptamine Schiff base in surfactant solubilized water pools in heptane - a fluorescence study. J. Photochem. Photobiol. B: Biol. 30, 273-307.
    • (1995) J. Photochem. Photobiol. B: Biol. , vol.30 , pp. 273-307
    • Singh, A.K.1    Majumdar, N.2
  • 26
    • 0033537884 scopus 로고    scopus 로고
    • Stoichiometry of a ligand-gated ion channel determined by fluorescence energy transfer
    • Farrar, S. J., P. J. Whitting, T. P. Bonnert, and R. M. McKernan (1999) Stoichiometry of a ligand-gated ion channel determined by fluorescence energy transfer. J. Biol. Chem. 274, 10100-10104.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10100-10104
    • Farrar, S.J.1    Whitting, P.J.2    Bonnert, T.P.3    McKernan, R.M.4
  • 27
    • 0032787283 scopus 로고    scopus 로고
    • Structure of cytochrome c complexes with phospholipids as revealed by resonance energy transfer
    • Gorbenko, G. P. (1999) Structure of cytochrome c complexes with phospholipids as revealed by resonance energy transfer. Biochim. Biophys. Acta 1420, 1-13.
    • (1999) Biochim. Biophys. Acta , vol.1420 , pp. 1-13
    • Gorbenko, G.P.1
  • 28
    • 0031664283 scopus 로고    scopus 로고
    • Fluorescence energy transfer of complexes of skeletal muscle troponin c and melittin derivatives
    • Sano, H., S. Takahashi, and T. Iio (1999) Fluorescence energy transfer of complexes of skeletal muscle troponin c and melittin derivatives. J. Biochem. 124, 602-604.
    • (1999) J. Biochem. , vol.124 , pp. 602-604
    • Sano, H.1    Takahashi, S.2    Iio, T.3
  • 29
    • 0032479355 scopus 로고    scopus 로고
    • Subunit exchange of lens alpha-crystallin - A fluorescence energy transfer study with the fluorescent labeled alpha-crystallin mutant W9F as a probe
    • Sun, T. X., N. J. Akhtar and J. J. N. Liang (1998) Subunit exchange of lens alpha-crystallin - a fluorescence energy transfer study with the fluorescent labeled alpha-crystallin mutant W9F as a probe. FEBS Lett. 430, 401-404.
    • (1998) FEBS Lett. , vol.430 , pp. 401-404
    • Sun, T.X.1    Akhtar, N.J.2    Liang, J.J.N.3
  • 30
    • 0029860227 scopus 로고    scopus 로고
    • Fluorescence energy transfer measurement of distances between ligand binding sites of tubulin and its implication for protein-protein interaction
    • Bhattacharya, A., B. Bhattacharya and S. Roy (1996) Fluorescence energy transfer measurement of distances between ligand binding sites of tubulin and its implication for protein-protein interaction. Protein Sci. 5, 2029-2036.
    • (1996) Protein Sci. , vol.5 , pp. 2029-2036
    • Bhattacharya, A.1    Bhattacharya, B.2    Roy, S.3
  • 31
    • 0033514429 scopus 로고    scopus 로고
    • Fluorescence energy transfer as a probe for tetraplex formation: The i-motif
    • Mergny, J. L. (1999) Fluorescence energy transfer as a probe for tetraplex formation: the i-motif. Biochemistry 38, 1573-1581.
    • (1999) Biochemistry , vol.38 , pp. 1573-1581
    • Mergny, J.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.