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Volumn 83, Issue 4, 2002, Pages 2231-2239

Binding of cations of group IA and IIA to bovine serum amine oxidase: Effect on the activity

Author keywords

[No Author keywords available]

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); CALCIUM ION; CATION; CESIUM ION; MAGNESIUM ION; POTASSIUM ION; SODIUM ION;

EID: 0036788551     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(02)73983-0     Document Type: Article
Times cited : (12)

References (36)
  • 1
    • 0030032121 scopus 로고    scopus 로고
    • Inorganic, monovalent cations compete with agonists for the transmitter binding site of nicotinic acetylcholine receptors
    • Akk, G., and A. Auerbach. 1996. Inorganic, monovalent cations compete with agonists for the transmitter binding site of nicotinic acetylcholine receptors. Biophys. J. 70:2652-2658.
    • (1996) Biophys. J. , vol.70 , pp. 2652-2658
    • Akk, G.1    Auerbach, A.2
  • 3
    • 0010559139 scopus 로고
    • Equilibrium electrochemistry: Ions and electrodes
    • Oxford University Press, Oxford
    • Atkins, P. W. 1986. Equilibrium electrochemistry: ions and electrodes. In Physical Chemistry, 3rd ed. Oxford University Press, Oxford. 237-245.
    • (1986) Physical Chemistry, 3rd ed. , pp. 237-245
    • Atkins, P.W.1
  • 4
    • 0027982961 scopus 로고
    • Structure and selectivity of monovalent cation binding site in cubic insulin crystals
    • Badger, J., A. Kapulsky, O. Gursky, B. Bhyravbhatla, and D. L. D. Caspar. 1994. Structure and selectivity of monovalent cation binding site in cubic insulin crystals. Biophys. J. 66:286-292.
    • (1994) Biophys. J. , vol.66 , pp. 286-292
    • Badger, J.1    Kapulsky, A.2    Gursky, O.3    Bhyravbhatla, B.4    Caspar, D.L.D.5
  • 5
    • 0015595680 scopus 로고
    • Kinetic of the diamino oxidase reaction
    • Bardsley, W. G., M. J. C. Crabbe, and J. Shindel. 1973. Kinetic of the diamino oxidase reaction. Biochem. J. 131:459-469.
    • (1973) Biochem. J. , vol.131 , pp. 459-469
    • Bardsley, W.G.1    Crabbe, M.J.C.2    Shindel, J.3
  • 6
    • 0000767958 scopus 로고
    • Relative binding affinities of monovalent cations for double-stranded DNA
    • Bleam, M. L., C. F. Anderson, and M. T. Record, Jr. 1980. Relative binding affinities of monovalent cations for double-stranded DNA. Proc. Natl. Acad. Sci. U.S.A. 77:3085-3089.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 3085-3089
    • Bleam, M.L.1    Anderson, C.F.2    Record M.T., Jr.3
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0010595491 scopus 로고
    • Precipitation and the solubility product
    • Addison Wesley, London
    • Butler, J. N. 1964. Precipitation and the solubility product. In Ionic Equilibrium: A Mathematical Approach. Addison Wesley, London. 292-295.
    • (1964) Ionic Equilibrium: A Mathematical Approach , pp. 292-295
    • Butler, J.N.1
  • 10
  • 11
    • 0028202998 scopus 로고
    • A sensilive spectrophotometry-based method for the determination of the rate of hydrogen peroxide generation in biological systems
    • Di Paolo, M. L., M. Scarpa, and A. Rigo. 1994. A sensilive spectrophotometry-based method for the determination of the rate of hydrogen peroxide generation in biological systems. J. Biochem. Biophys. Methods. 28:205-214.
    • (1994) J. Biochem. Biophys. Methods , vol.28 , pp. 205-214
    • Di Paolo, M.L.1    Scarpa, M.2    Rigo, A.3
  • 12
    • 77049143386 scopus 로고
    • The determination of enzyme inhibition constants
    • Dixon, M. 1953. The determination of enzyme inhibition constants. Biochem. J. 55:170-171.
    • (1953) Biochem. J. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 13
    • 0002864801 scopus 로고
    • On the elementary atomic origin of ionic specificity
    • A. Kleinzeller and L. Kotyk, editors. Academic Press, New York
    • Eisenman, G. 1961. On the elementary atomic origin of ionic specificity In Symposium on Membrane Transport and Metabolism. A. Kleinzeller and L. Kotyk, editors. Academic Press, New York. 163-179.
    • (1961) Symposium on Membrane Transport and Metabolism , pp. 163-179
    • Eisenman, G.1
  • 14
    • 0022500259 scopus 로고
    • pH dependence of deuterium isotopic effects and tritium exchange in the bovine plasma amine oxidase reaction: A role for single base catalysis in amine oxidation and imine exchange
    • Farnun, M., M. Palcic, and J. P. Klinman. 1986. pH dependence of deuterium isotopic effects and tritium exchange in the bovine plasma amine oxidase reaction: a role for single base catalysis in amine oxidation and imine exchange. Biochemistry. 25:1898-1904.
    • (1986) Biochemistry , vol.25 , pp. 1898-1904
    • Farnun, M.1    Palcic, M.2    Klinman, J.P.3
  • 15
  • 16
    • 0001166155 scopus 로고
    • Amine oxidases
    • H. Sigel and A. Sigel, editors. Dekker, New York
    • Knowles, P. F., and D. M. Dooley. 1994. Amine oxidases. In Metal Ions in Biological Systems, Vol. 30. H. Sigel and A. Sigel, editors. Dekker, New York. 361-403.
    • (1994) Metal Ions in Biological Systems , vol.30 , pp. 361-403
    • Knowles, P.F.1    Dooley, D.M.2
  • 18
    • 0027999913 scopus 로고
    • Influence of monovalent cations on the ultraviolet-visible spectrum of tryptophan tryptophylquinone-containing methylamine dehydrogenase from bacterium W3A1
    • Kuusk, V., and W. S. McIntire. 1994. Influence of monovalent cations on the ultraviolet-visible spectrum of tryptophan tryptophylquinone-containing methylamine dehydrogenase from bacterium W3A1. J. Biol. Chem. 269:26136-26143.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26136-26143
    • Kuusk, V.1    McIntire, W.S.2
  • 20
    • 0000566343 scopus 로고
    • Limiting laws and counterion condensation in polyelectrolyte solutions. VIII. Mixtures of counterions, species selectivity and valence selectivity
    • Manning, G. S. 1984. Limiting laws and counterion condensation in polyelectrolyte solutions. VIII. Mixtures of counterions, species selectivity and valence selectivity. J. Phys. Chem. 88:6654-6661.
    • (1984) J. Phys. Chem. , vol.88 , pp. 6654-6661
    • Manning, G.S.1
  • 22
    • 0015693284 scopus 로고
    • High-resolution proton magnetic resonance studies of two trypsin inhibitors: Soybean trypsin inhibitor (Kunitz) and ovomucoid (hen egg white)
    • Markley, J. 1973. High-resolution proton magnetic resonance studies of two trypsin inhibitors: soybean trypsin inhibitor (Kunitz) and ovomucoid (hen egg white). Ann. N.Y. Acad. Sci. 222:347-373.
    • (1973) Ann. N.Y. Acad. Sci. , vol.222 , pp. 347-373
    • Markley, J.1
  • 24
    • 0033614821 scopus 로고    scopus 로고
    • The active site base controls cofactor reactivity in Escherichia coli amine oxidase: X-ray crystallographic studies with mutational variants
    • Murray, J. M., C. G. Saysell, M. C. Wilmot, W. S. Tambyrajah, J. Jaeger, P. F. Knowles, E. E. V. Philips, and M. J. McPherson. 1999. The active site base controls cofactor reactivity in Escherichia coli amine oxidase: x-ray crystallographic studies with mutational variants. Biochemistry. 38:8217-8227.
    • (1999) Biochemistry , vol.38 , pp. 8217-8227
    • Murray, J.M.1    Saysell, C.G.2    Wilmot, M.C.3    Tambyrajah, W.S.4    Jaeger, J.5    Knowles, P.F.6    Philips, E.E.V.7    McPherson, M.J.8
  • 27
    • 0033614781 scopus 로고    scopus 로고
    • An unexpected role for the active site base in cofactor orientation and flexibility in copper amine oxidase from Harsenula polymorpha
    • Plastino, J. E. L. Green, J. Sanders-Loehr. and J. P. Klinman. 1999. An unexpected role for the active site base in cofactor orientation and flexibility in copper amine oxidase from Harsenula polymorpha. Biochemistry. 38:8204-8216.
    • (1999) Biochemistry , vol.38 , pp. 8204-8216
    • Plastino, J.E.1    Green, L.2    Sanders-Loehr, J.3    Klinman, J.P.4
  • 28
    • 85031445544 scopus 로고
    • Calculation of bandshapes of first-order NMR spectra: The modified Bloch equations
    • Academic Press, London
    • Sanström, J. 1982. Calculation of bandshapes of first-order NMR spectra: the modified Bloch equations. In Dynamic NMR Spectroscopy. Academic Press, London. 12-18.
    • (1982) Dynamic NMR Spectroscopy , pp. 12-18
    • Sanström, J.1
  • 29
    • 0030831696 scopus 로고    scopus 로고
    • Confirmation of the presence of a Cu(II)/topaquinone active site in the amine oxidase from fenugreek seedlings
    • Sebela, M., L. Luhova, I. Frebort, S. Hirota, H. G. Faulhammer, V. Stuzka, and P. Pec. 1997. Confirmation of the presence of a Cu(II)/topaquinone active site in the amine oxidase from fenugreek seedlings. J. Exp. Bot. 48:1897-1907.
    • (1997) J. Exp. Bot. , vol.48 , pp. 1897-1907
    • Sebela, M.1    Luhova, L.2    Frebort, I.3    Hirota, S.4    Faulhammer, H.G.5    Stuzka, V.6    Pec, P.7
  • 31
    • 0028258569 scopus 로고
    • Electrostatic control of oxidative deamination catalysed by bovine serum amine oxidase
    • Stevanato, R., B. Mondovi, O. Befani, M. Scarpa, and A. Rigo. 1994. Electrostatic control of oxidative deamination catalysed by bovine serum amine oxidase. Biochem. J. 299:317-320.
    • (1994) Biochem. J. , vol.299 , pp. 317-320
    • Stevanato, R.1    Mondovi, B.2    Befani, O.3    Scarpa, M.4    Rigo, A.5
  • 32
    • 0029040435 scopus 로고
    • Cloning and molecular analysis of the pea seedling copper amine oxidase
    • Tipping, A. J., and M. J. McPherson. 1995. Cloning and molecular analysis of the pea seedling copper amine oxidase. J. Biol. Chem. 270: 16939-16946.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16939-16946
    • Tipping, A.J.1    McPherson, M.J.2
  • 34
    • 0031414412 scopus 로고    scopus 로고
    • Crystal structure of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: Implications for the biogenesis of topaquinone
    • Wilce, M. C. J., D. M. Dooley, H. C. Freeman, J. M. Guss, H. Matsunami, W. S. McIntire, C. E. Ruggiero, K. Tanizawa, and H. Yamaguchi. 1997. Crystal structure of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone. Biochemistry. 36:16116-16133.
    • (1997) Biochemistry , vol.36 , pp. 16116-16133
    • Wilce, M.C.J.1    Dooley, D.M.2    Freeman, H.C.3    Guss, J.M.4    Matsunami, H.5    McIntire, W.S.6    Ruggiero, C.E.7    Tanizawa, K.8    Yamaguchi, H.9
  • 35
    • 0000023373 scopus 로고
    • Colorimetric determination of calcium with ammonium purpurate
    • Williams, M. B., and J. H. Moser. 1953. Colorimetric determination of calcium with ammonium purpurate. Anal. Chem. 25:1414-1417.
    • (1953) Anal. Chem. , vol.25 , pp. 1414-1417
    • Williams, M.B.1    Moser, J.H.2
  • 36
    • 0035868945 scopus 로고    scopus 로고
    • 2-Bromoethylamine as a potent selective suicide inhibitor for semicarbazide-sensitive amine oxidase
    • Yu, P. H., B. A. Davis, and Y. Deng. 2001. 2-Bromoethylamine as a potent selective suicide inhibitor for semicarbazide-sensitive amine oxidase. Biochem. Pharmacol. 61:741-748.
    • (2001) Biochem. Pharmacol. , vol.61 , pp. 741-748
    • Yu, P.H.1    Davis, B.A.2    Deng, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.