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Volumn 44, Issue 6, 2005, Pages 1864-1871

Metal ion binding to human hemopexin

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; CHARGED PARTICLES; IONS; ISOTHERMS; MANGANESE COMPOUNDS; NICKEL COMPOUNDS; RESINS; SPECTRUM ANALYSIS; TITRATION; ZINC COMPOUNDS;

EID: 13544267446     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0481747     Document Type: Article
Times cited : (31)

References (57)
  • 1
    • 0018082852 scopus 로고
    • Transport of heme by hemopexin to the liver: Evidence for receptor-mediated uptake
    • Smith, A., and Morgan, W. T. (1978) Transport of heme by hemopexin to the liver: Evidence for receptor-mediated uptake, Biochem. Biophys. Res. Commun. 84, 151-157.
    • (1978) Biochem. Biophys. Res. Commun. , vol.84 , pp. 151-157
    • Smith, A.1    Morgan, W.T.2
  • 2
    • 0018634705 scopus 로고
    • Haem transport to the liver by haemopexin. Receptor-mediated uptake with recycling of the protein
    • Smith, A., and Morgan, W. T. (1979) Haem transport to the liver by haemopexin. Receptor-mediated uptake with recycling of the protein, Biochem. J. 182, 47-54.
    • (1979) Biochem. J. , vol.182 , pp. 47-54
    • Smith, A.1    Morgan, W.T.2
  • 3
    • 0028792111 scopus 로고
    • Lipid peroxidation and antioxidants as biomarkers of tissue damage
    • Gutteridge, J. M. (1995) Lipid peroxidation and antioxidants as biomarkers of tissue damage, Clin. Chem. 41, 1819-1828.
    • (1995) Clin. Chem. , vol.41 , pp. 1819-1828
    • Gutteridge, J.M.1
  • 4
    • 0032800507 scopus 로고    scopus 로고
    • The effects of heme-binding proteins on the peroxidative and catalatic activities of hemin
    • Grinberg, L. N., O'Brien, P. J., and Hrkal, Z. (1999) The effects of heme-binding proteins on the peroxidative and catalatic activities of hemin, Free Radical Biol. Med. 27, 214-219.
    • (1999) Free Radical Biol. Med. , vol.27 , pp. 214-219
    • Grinberg, L.N.1    O'Brien, P.J.2    Hrkal, Z.3
  • 5
    • 0036259938 scopus 로고    scopus 로고
    • Hemopexin: Structure, function, and regulation
    • Tolosano, E., and Altruda, F. (2002) Hemopexin: Structure, function, and regulation, DNA Cell Biol. 21, 297-306.
    • (2002) DNA Cell Biol. , vol.21 , pp. 297-306
    • Tolosano, E.1    Altruda, F.2
  • 6
    • 0034806977 scopus 로고    scopus 로고
    • Hemopexin: A review of biological aspects and the role in laboratory medicine
    • Delanghe, J. R., and Langlois, M. R. (2001) Hemopexin: A review of biological aspects and the role in laboratory medicine, Clin. Chim. Acta 312, 13-23.
    • (2001) Clin. Chim. Acta , vol.312 , pp. 13-23
    • Delanghe, J.R.1    Langlois, M.R.2
  • 7
    • 0011045635 scopus 로고    scopus 로고
    • Binding and transport of iron-porphyrins by hemopexin
    • Morgan, W. T., and Smith, A. (2000) Binding and transport of iron-porphyrins by hemopexin, Adv. Inorg. Chem. 51, 205-241.
    • (2000) Adv. Inorg. Chem. , vol.51 , pp. 205-241
    • Morgan, W.T.1    Smith, A.2
  • 8
    • 0032825215 scopus 로고    scopus 로고
    • Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two β-propeller domains
    • Paoli, M., Anderson, B. F., Baker, H. M., Morgan, W. T., Smith, A., and Baker, E. N. (1999) Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two β-propeller domains, Nat. Struct. Biol. 6, 926-931.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 926-931
    • Paoli, M.1    Anderson, B.F.2    Baker, H.M.3    Morgan, W.T.4    Smith, A.5    Baker, E.N.6
  • 9
    • 0033947801 scopus 로고    scopus 로고
    • Links between cell-surface events involving redox-active copper and gene regulation in the hemopexin heme transport system
    • Smith, A. (2000) Links between cell-surface events involving redox-active copper and gene regulation in the hemopexin heme transport system, Antioxid. Redox Signal. 2, 157-175.
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 157-175
    • Smith, A.1
  • 10
    • 0027186588 scopus 로고
    • Characterization of hemopexin and its interaction with heme by differential scanning calorimetry and circular dichroism
    • Wu, M. L., and Morgan, W. T. (1993) Characterization of hemopexin and its interaction with heme by differential scanning calorimetry and circular dichroism, Biochemistry 32, 7216-7222.
    • (1993) Biochemistry , vol.32 , pp. 7216-7222
    • Wu, M.L.1    Morgan, W.T.2
  • 11
    • 0028948672 scopus 로고
    • Thermodynamics of heme-induced conformational changes in hemopexin: Role of domain-domain interactions
    • Wu, M. L., and Morgan, W. T. (1995) Thermodynamics of heme-induced conformational changes in hemopexin: Role of domain-domain interactions, Protein Sci. 4, 29-34.
    • (1995) Protein Sci. , vol.4 , pp. 29-34
    • Wu, M.L.1    Morgan, W.T.2
  • 13
    • 0021114727 scopus 로고
    • Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions
    • Porath, J., and Olin, B. (1983) Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions, Biochemistry 22, 1621-1630.
    • (1983) Biochemistry , vol.22 , pp. 1621-1630
    • Porath, J.1    Olin, B.2
  • 14
    • 0021647404 scopus 로고
    • Fractionation of human serum proteins by immobilized metal affinity chromatography
    • Andersson, L. (1984) Fractionation of human serum proteins by immobilized metal affinity chromatography, J. Chromatogr. 315, 167-174.
    • (1984) J. Chromatogr. , vol.315 , pp. 167-174
    • Andersson, L.1
  • 15
    • 0020822727 scopus 로고
    • Immobilized-metal affinity chromatography of serum proteins on gel-immobilized group III A metal ions
    • Porath, J., Olin, B., and Granstrand, B. (1983) Immobilized-metal affinity chromatography of serum proteins on gel-immobilized group III A metal ions, Arch. Biochem. Biophys. 225, 543-547.
    • (1983) Arch. Biochem. Biophys. , vol.225 , pp. 543-547
    • Porath, J.1    Olin, B.2    Granstrand, B.3
  • 17
    • 0026179732 scopus 로고
    • Further characterization of carboxymethylated aspartic acid agarose. Purification of human α-2-macroglobulin and hemopexin
    • Mantovaara, T., Pertoft, H., and Porath, J. (1991) Further characterization of carboxymethylated aspartic acid agarose. Purification of human α-2-macroglobulin and hemopexin, Biotechnol. Appl. Biochem. 13, 371-379.
    • (1991) Biotechnol. Appl. Biochem. , vol.13 , pp. 371-379
    • Mantovaara, T.1    Pertoft, H.2    Porath, J.3
  • 18
    • 0032054959 scopus 로고    scopus 로고
    • Characterization of trout serum hemopexin through the use of a recombinant protein
    • de Monti, M., Miot, S., Le Goff, P., and Duval, J. (1998) Characterization of trout serum hemopexin through the use of a recombinant protein, C. R. Seances Acad. Sci., Ser. III 321, 299-304.
    • (1998) C. R. Seances Acad. Sci., Ser. III , vol.321 , pp. 299-304
    • De Monti, M.1    Miot, S.2    Le Goff, P.3    Duval, J.4
  • 19
    • 0017074206 scopus 로고
    • A solvent system for delipidation of plasma or serum without protein precipitation
    • Cham, B. E., and Knowles, B. R. (1976) A solvent system for delipidation of plasma or serum without protein precipitation, J. Lipid Res. 17, 176-181.
    • (1976) J. Lipid Res. , vol.17 , pp. 176-181
    • Cham, B.E.1    Knowles, B.R.2
  • 20
    • 0015335301 scopus 로고
    • Hemopexin of human and rabbit: Molecular weight and extinction coefficient
    • Seery, V. L., Hathaway, G., and Müller-Eberhard, U. (1972) Hemopexin of human and rabbit: Molecular weight and extinction coefficient, Arch. Biochem. Biophys. 150, 269-272.
    • (1972) Arch. Biochem. Biophys. , vol.150 , pp. 269-272
    • Seery, V.L.1    Hathaway, G.2    Müller-Eberhard, U.3
  • 21
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling, Biophys. J. 78, 1606-1619.
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 23
    • 0015437961 scopus 로고
    • Study of protein-protein and of protein-ligand interactions by potentiometric methods
    • Laskowski, M., and Finkenstadt, W. R. (1972) Study of protein-protein and of protein-ligand interactions by potentiometric methods, Methods Enzymol. 26, 193-277.
    • (1972) Methods Enzymol. , vol.26 , pp. 193-277
    • Laskowski, M.1    Finkenstadt, W.R.2
  • 24
    • 0026091157 scopus 로고
    • 5: Electrostatic consequences of protein-protein interactions
    • 5: Electrostatic consequences of protein-protein interactions, Biochemistry 30, 9873-9881.
    • (1991) Biochemistry , vol.30 , pp. 9873-9881
    • Mauk, M.R.1    Barker, P.D.2    Mauk, A.G.3
  • 25
    • 0028062898 scopus 로고
    • Proton linkage in formation of the cytochrome c-cytochrome c peroxidase complex: Electrostatic properties of the high- and low-affinity cytochrome binding sites on the peroxidase
    • Mauk, M. R., Ferrer, J. C., and Mauk, A. G. (1994) Proton linkage in formation of the cytochrome c-cytochrome c peroxidase complex: Electrostatic properties of the high- and low-affinity cytochrome binding sites on the peroxidase, Biochemistry 33, 12609-12614.
    • (1994) Biochemistry , vol.33 , pp. 12609-12614
    • Mauk, M.R.1    Ferrer, J.C.2    Mauk, A.G.3
  • 26
    • 49049126489 scopus 로고
    • Efficient detection of paramagnetically shifted NMR resonances by optimizing the WEFT pulse sequence
    • Inubushi, T., and Becker, E. D. (1983) Efficient detection of paramagnetically shifted NMR resonances by optimizing the WEFT pulse sequence, J. Magn. Reson. 51, 128-133.
    • (1983) J. Magn. Reson. , vol.51 , pp. 128-133
    • Inubushi, T.1    Becker, E.D.2
  • 28
    • 0016259907 scopus 로고
    • Human hemopexin. Preparation and magnetic properties
    • Aisen, P., Leibman, A., Harris, D. C., and Moss, T. (1974) Human hemopexin. Preparation and magnetic properties, J. Biol. Chem. 249, 6824-6827.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6824-6827
    • Aisen, P.1    Leibman, A.2    Harris, D.C.3    Moss, T.4
  • 29
    • 0014138625 scopus 로고
    • Purification and partial characterization of human hemopexin
    • Müller-Eberhard, U., and English, E. C. (1967) Purification and partial characterization of human hemopexin, J. Lab. Clin. Med. 70, 619-626.
    • (1967) J. Lab. Clin. Med. , vol.70 , pp. 619-626
    • Müller-Eberhard, U.1    English, E.C.2
  • 30
    • 0015219585 scopus 로고
    • Partial characterization of the heme-binding serum glycoproteins rabbit and human hemopexin
    • Hrkal, Z., and Müller-Eberhard, U. (1971) Partial characterization of the heme-binding serum glycoproteins rabbit and human hemopexin, Biochemistry 10, 1746-1750.
    • (1971) Biochemistry , vol.10 , pp. 1746-1750
    • Hrkal, Z.1    Müller-Eberhard, U.2
  • 32
    • 0023623557 scopus 로고
    • Genetic studies of low-abundance human plasma proteins. VI. Polymorphism of hemopexin
    • Kamboh, M. I., and Ferrell, R. E. (1987) Genetic studies of low-abundance human plasma proteins. VI. Polymorphism of hemopexin, Am. J. Hum. Genet. 41, 645-653.
    • (1987) Am. J. Hum. Genet. , vol.41 , pp. 645-653
    • Kamboh, M.I.1    Ferrell, R.E.2
  • 33
    • 0002656925 scopus 로고
    • Structure of human hemopexin: O-Glycosyl and N-glycosyl sites and unusual clustering of tryptophan residues
    • Takahashi, N., Takahashi, Y., and Putnam, F. W. (1984) Structure of human hemopexin: O-Glycosyl and N-glycosyl sites and unusual clustering of tryptophan residues, Proc. Natl. Acad. Sci. U.S.A. 81, 2021-2025.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 2021-2025
    • Takahashi, N.1    Takahashi, Y.2    Putnam, F.W.3
  • 34
    • 0028834595 scopus 로고
    • MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domain
    • Cox, M. C., Le Brun, N., Thomson, A. J., Smith, A., Morgan, W. T., and Moore, G. R. (1995) MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domain, Biochim. Biophys. Acta 1253, 215-223.
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 215-223
    • Cox, M.C.1    Le Brun, N.2    Thomson, A.J.3    Smith, A.4    Morgan, W.T.5    Moore, G.R.6
  • 36
    • 0002228715 scopus 로고    scopus 로고
    • NMR of paramagnetic substances
    • Bertini, I., and Luchinat, C. (1996) NMR of paramagnetic substances, Coord. Chem. Rev. 150, 1-296.
    • (1996) Coord. Chem. Rev. , vol.150 , pp. 1-296
    • Bertini, I.1    Luchinat, C.2
  • 39
    • 0037623317 scopus 로고    scopus 로고
    • Molecular mechanisms and regulation of iron transport
    • Chung, J., and Wessling-Resnick, M. (2003) Molecular mechanisms and regulation of iron transport, Crit. Rev. Clin. Lab. Sci. 40, 151-182.
    • (2003) Crit. Rev. Clin. Lab. Sci. , vol.40 , pp. 151-182
    • Chung, J.1    Wessling-Resnick, M.2
  • 40
    • 0025376223 scopus 로고
    • Binding of Cu(II) to non-prosthetic sites in ceruloplasmin and bovine serum albumin
    • Zgirski, A., and Frieden, E. (1990) Binding of Cu(II) to non-prosthetic sites in ceruloplasmin and bovine serum albumin, J. Inorg. Biochem. 39, 137-148.
    • (1990) J. Inorg. Biochem. , vol.39 , pp. 137-148
    • Zgirski, A.1    Frieden, E.2
  • 41
    • 0019871890 scopus 로고
    • Interactions of the histidine-rich glycoprotein of serum with metals
    • Morgan, W. T. (1981) Interactions of the histidine-rich glycoprotein of serum with metals, Biochemistry 20, 1054-1061.
    • (1981) Biochemistry , vol.20 , pp. 1054-1061
    • Morgan, W.T.1
  • 42
    • 0022423906 scopus 로고
    • The histidine-rich glycoprotein of serum has a domain rich in histidine, proline, and glycine that binds heme and metals
    • Morgan, W. T. (1985) The histidine-rich glycoprotein of serum has a domain rich in histidine, proline, and glycine that binds heme and metals, Biochemistry 24, 1496-1501.
    • (1985) Biochemistry , vol.24 , pp. 1496-1501
    • Morgan, W.T.1
  • 43
    • 0033545342 scopus 로고    scopus 로고
    • Acute-phase proteins and other systemic responses to inflammation
    • Gabay, C., and Kushner, I. (1999) Acute-phase proteins and other systemic responses to inflammation, N. Engl. J. Med. 340, 448-454.
    • (1999) N. Engl. J. Med. , vol.340 , pp. 448-454
    • Gabay, C.1    Kushner, I.2
  • 44
    • 0000844197 scopus 로고
    • Surface topography of histidine residues: A facile probe by immobilized metal ion affinity chromatography
    • Hemdan, E. S., Zhao, Y. J., Sulkowski, E., and Porath, J. (1989) Surface topography of histidine residues: A facile probe by immobilized metal ion affinity chromatography, Proc. Natl. Acad. Sci. U.S.A. 86, 1811-1815.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 1811-1815
    • Hemdan, E.S.1    Zhao, Y.J.2    Sulkowski, E.3    Porath, J.4
  • 45
    • 0033492499 scopus 로고    scopus 로고
    • Comparison of different transition metal ions for immobilized metal affinity chromatography of selenoprotein P from human plasma
    • Sidenius, U., Farver, O., Jons, O., and Gammelgaard, B. (1999) Comparison of different transition metal ions for immobilized metal affinity chromatography of selenoprotein P from human plasma, J. Chromatogr., B: Biomed. Sci. Appl. 735, 85-91.
    • (1999) J. Chromatogr., B: Biomed. Sci. Appl. , vol.735 , pp. 85-91
    • Sidenius, U.1    Farver, O.2    Jons, O.3    Gammelgaard, B.4
  • 46
    • 0000123474 scopus 로고
    • 1H NMR spectra of the coordination sphere of cobalt-substituted carbonic anhydrase
    • 1H NMR spectra of the coordination sphere of cobalt-substituted carbonic anhydrase, J. Am. Chem. Soc. 103, 7784-7788.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 7784-7788
    • Bertini, I.1    Canti, G.2    Luchinat, C.3    Mani, F.4
  • 47
    • 0020406955 scopus 로고
    • High-resolution proton nuclear magnetic resonance studies of the nickel(II) derivative of azurin
    • Blaszak, J. A., Ulrich, E. L., Markley, J. L., and McMillin, D. R. (1982) High-resolution proton nuclear magnetic resonance studies of the nickel(II) derivative of azurin, Biochemistry 21, 6253-6258.
    • (1982) Biochemistry , vol.21 , pp. 6253-6258
    • Blaszak, J.A.1    Ulrich, E.L.2    Markley, J.L.3    McMillin, D.R.4
  • 48
    • 2542494507 scopus 로고    scopus 로고
    • EPR and magnetic susceptibility studies of cobalt(II)- and nickel(II)-substituted azurins from Pseudomonas aeruginosa. Electronic structure of the active sites
    • Jimenez, H. R., Salgado, J., Moratal, J. M., and Morgenstern-Badarau, I. (1996) EPR and magnetic susceptibility studies of cobalt(II)- and nickel(II)-substituted azurins from Pseudomonas aeruginosa. Electronic structure of the active sites, Inorg. Chem. 35, 2737-2741.
    • (1996) Inorg. Chem. , vol.35 , pp. 2737-2741
    • Jimenez, H.R.1    Salgado, J.2    Moratal, J.M.3    Morgenstern-Badarau, I.4
  • 50
    • 0031837179 scopus 로고    scopus 로고
    • Effect of nickel(II) substitution on the resonance Raman and NMR spectra of Alcaligenes xylosoxidans azurin II: Implications for axial-ligand bonding interactions in cupredoxin active sites
    • Hannan, J. P., Davy, S. L., Moore, G. R., Eady, R. R., and Andrew, C. R. (1998) Effect of nickel(II) substitution on the resonance Raman and NMR spectra of Alcaligenes xylosoxidans azurin II: Implications for axial-ligand bonding interactions in cupredoxin active sites, J. Biol. Inorg. Chem. 3, 282-291.
    • (1998) J. Biol. Inorg. Chem. , vol.3 , pp. 282-291
    • Hannan, J.P.1    Davy, S.L.2    Moore, G.R.3    Eady, R.R.4    Andrew, C.R.5
  • 51
    • 0036135474 scopus 로고    scopus 로고
    • Binding ability of sialic acid towards biological and toxic metal ions. NMR, potentiometric and spectroscopic study
    • Saladini, M., Menabue, L., and Ferrari, E. (2002) Binding ability of sialic acid towards biological and toxic metal ions. NMR, potentiometric and spectroscopic study, J. Inorg. Biochem. 88, 61-68.
    • (2002) J. Inorg. Biochem. , vol.88 , pp. 61-68
    • Saladini, M.1    Menabue, L.2    Ferrari, E.3
  • 52
    • 0033847193 scopus 로고    scopus 로고
    • Heme binding by hemopexin: Evidence for multiple modes of binding and functional implications
    • Shipulina, N., Smith, A., and Morgan, W. T. (2000) Heme binding by hemopexin: Evidence for multiple modes of binding and functional implications, J. Protein Chem. 19, 239-248.
    • (2000) J. Protein Chem. , vol.19 , pp. 239-248
    • Shipulina, N.1    Smith, A.2    Morgan, W.T.3
  • 53
    • 0017845559 scopus 로고
    • Magnetic and natural circular dichroism of metalloporphyrin complexes of human and rabbit hemopexin
    • Morgan, W. T., and Vickery, L. E. (1978) Magnetic and natural circular dichroism of metalloporphyrin complexes of human and rabbit hemopexin, J. Biol. Chem. 253, 2940-2945.
    • (1978) J. Biol. Chem. , vol.253 , pp. 2940-2945
    • Morgan, W.T.1    Vickery, L.E.2
  • 54
    • 0027199762 scopus 로고
    • Optical activity of hemoproteins in the Soret region. Circular dichroism of the heme undecapeptide of cytochrome c in aqueous solution
    • Blauer, G., Sreerama, N., and Woody, R. W. (1993) Optical activity of hemoproteins in the Soret region. Circular dichroism of the heme undecapeptide of cytochrome c in aqueous solution, Biochemistry 32, 6674-6679.
    • (1993) Biochemistry , vol.32 , pp. 6674-6679
    • Blauer, G.1    Sreerama, N.2    Woody, R.W.3
  • 55
    • 0037388042 scopus 로고    scopus 로고
    • Dealing with iron: Common structural principles in proteins that transport iron and heme
    • Baker, H. M., Anderson, B. F., and Baker, E. N. (2003) Dealing with iron: Common structural principles in proteins that transport iron and heme, Proc. Natl. Acad. Sci. U.S.A. 100, 3579-3583.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3579-3583
    • Baker, H.M.1    Anderson, B.F.2    Baker, E.N.3
  • 57
    • 0014409091 scopus 로고
    • Conformation of cytochromes. II. Comparative study of circular dichroism spectra, optical rotatory dispersion, and absorption spectra of horse heart cytochrome c
    • Myer, Y. P. (1968) Conformation of cytochromes. II. Comparative study of circular dichroism spectra, optical rotatory dispersion, and absorption spectra of horse heart cytochrome c, J. Biol. Chem. 243, 2115-2122.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2115-2122
    • Myer, Y.P.1


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