메뉴 건너뛰기




Volumn 46, Issue 51, 2007, Pages 15033-15041

Chromatographically distinguishable heme insertion isoforms of human hemopexin

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; BINDING SITES; METAL IONS; MOLECULAR INTERACTIONS; PLASMA (HUMAN);

EID: 37349037560     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701821a     Document Type: Article
Times cited : (8)

References (70)
  • 1
    • 0030031587 scopus 로고    scopus 로고
    • Specific expression in brain and liver driven by the hemopexin promoter in transgenic mice
    • Tolosano, E., Cutufia, M. A., Hirsch, E., Silengo, L., and Altruda, F. (1996) Specific expression in brain and liver driven by the hemopexin promoter in transgenic mice, Biochem. Biophys. Res. Commun. 218, 694-703.
    • (1996) Biochem. Biophys. Res. Commun , vol.218 , pp. 694-703
    • Tolosano, E.1    Cutufia, M.A.2    Hirsch, E.3    Silengo, L.4    Altruda, F.5
  • 2
    • 0011045635 scopus 로고    scopus 로고
    • Binding and transport of iron-porphyrins by hemopexin
    • Morgan, W. T., and Smith, A. (2001) Binding and transport of iron-porphyrins by hemopexin, Adv. Inorg. Chem. 51, 205-293.
    • (2001) Adv. Inorg. Chem , vol.51 , pp. 205-293
    • Morgan, W.T.1    Smith, A.2
  • 3
    • 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
  • 4
    • 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
  • 5
    • 34249804150 scopus 로고    scopus 로고
    • Structural modelling of metal ion binding to human haemopexin
    • Mauk, M. R., Rosell, F. I., and Mauk, A. G. (2007) Structural modelling of metal ion binding to human haemopexin, Nat. Prod. Rep. 24, 523-532.
    • (2007) Nat. Prod. Rep , vol.24 , pp. 523-532
    • Mauk, M.R.1    Rosell, F.I.2    Mauk, A.G.3
  • 6
    • 0035168441 scopus 로고    scopus 로고
    • Hemopexins suppress phorbol ester-induced necrosis of polymorphonuclear leucocytes
    • Suzuki, K., Kato, H., Sakuma, Y., and Namiki, H. (2001) Hemopexins suppress phorbol ester-induced necrosis of polymorphonuclear leucocytes, Cell Struct. Funct. 26, 235-241.
    • (2001) Cell Struct. Funct , vol.26 , pp. 235-241
    • Suzuki, K.1    Kato, H.2    Sakuma, Y.3    Namiki, H.4
  • 7
    • 0242441490 scopus 로고    scopus 로고
    • 2+-dependent adhesion of polymorphonuclear leukocytes by serum hemopexin: Differences in divalent-cation dependency of cell adhesion in the presence and absence of serum
    • 2+-dependent adhesion of polymorphonuclear leukocytes by serum hemopexin: Differences in divalent-cation dependency of cell adhesion in the presence and absence of serum, Cell Struct. Funct. 28, 243-253.
    • (2003) Cell Struct. Funct , vol.28 , pp. 243-253
    • Suzuki, K.1    Kobayashi, N.2    Doi, T.3    Hijikata, T.4    Machida, I.5    Namiki, H.6
  • 8
    • 0022377775 scopus 로고
    • Intracellular distribution of haem after uptake by different receptors. Haem-haemopexin and haem-asialo-haemopexin
    • Smith, A. (1985) Intracellular distribution of haem after uptake by different receptors. Haem-haemopexin and haem-asialo-haemopexin, Biochem. J. 231, 663-669.
    • (1985) Biochem. J , vol.231 , pp. 663-669
    • Smith, A.1
  • 9
    • 0025670315 scopus 로고
    • Hemopexin joins transferrin as representative members of a distinct class of receptor-mediated endocytic transport systems
    • Smith, A., and Hunt, R. C. (1990) Hemopexin joins transferrin as representative members of a distinct class of receptor-mediated endocytic transport systems, Eur. J. Cell Biol. 53, 234-245.
    • (1990) Eur. J. Cell Biol , vol.53 , pp. 234-245
    • Smith, A.1    Hunt, R.C.2
  • 11
    • 0029437791 scopus 로고
    • EPR studies on the effects of complexation of heme by hemopexin upon its reactions with organic peroxides
    • Timmins, G. S., Davies, M. J., Song, D. X., and Muller-Eberhard, U. (1995) EPR studies on the effects of complexation of heme by hemopexin upon its reactions with organic peroxides, Free Radic. Res. 23, 559-569.
    • (1995) Free Radic. Res , vol.23 , pp. 559-569
    • Timmins, G.S.1    Davies, M.J.2    Song, D.X.3    Muller-Eberhard, U.4
  • 12
    • 0015980699 scopus 로고
    • Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin
    • Hrkal, Z., Vodrazka, Z., and Kalousek, I. (1974) Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin, Eur. J. Biochem. 43, 73-78.
    • (1974) Eur. J. Biochem , vol.43 , pp. 73-78
    • Hrkal, Z.1    Vodrazka, Z.2    Kalousek, I.3
  • 13
    • 0032997659 scopus 로고    scopus 로고
    • Kinetics of hemin distribution in plasma reveals its role in lipoprotein oxidation
    • Miller, Y. I., and Shaklai, N. (1999) Kinetics of hemin distribution in plasma reveals its role in lipoprotein oxidation, Biochim. Biophys. Acta 1454, 153-164.
    • (1999) Biochim. Biophys. Acta , vol.1454 , pp. 153-164
    • Miller, Y.I.1    Shaklai, N.2
  • 14
    • 0017073110 scopus 로고
    • The aromatic and heme chromophores of rabbit hemopexin. Difference absorption and fluorescence spectra
    • Morgan, W. T., Sutor, R. P., and Müller-Eberhard, U. (1976) The aromatic and heme chromophores of rabbit hemopexin. Difference absorption and fluorescence spectra, Biochim. Biophys. Acta 434, 311-323.
    • (1976) Biochim. Biophys. Acta , vol.434 , pp. 311-323
    • Morgan, W.T.1    Sutor, R.P.2    Müller-Eberhard, U.3
  • 15
    • 0032825215 scopus 로고    scopus 로고
    • Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-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 beta-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
  • 18
    • 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
  • 19
    • 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
  • 20
    • 13544276819 scopus 로고    scopus 로고
    • pH- and metal ion-linked stability of the hemopexin-heme complex
    • Rosell, F. I., Mauk, M. R., and Mauk, A. G. (2005) pH- and metal ion-linked stability of the hemopexin-heme complex, Biochemistry 44, 1872-1879.
    • (2005) Biochemistry , vol.44 , pp. 1872-1879
    • Rosell, F.I.1    Mauk, M.R.2    Mauk, A.G.3
  • 21
    • 34547920004 scopus 로고    scopus 로고
    • Effects of metal ion binding on structural dynamics of human hemopexin
    • Rosell, F. I., Mauk, M. R., and Mauk, A. G. (2007) Effects of metal ion binding on structural dynamics of human hemopexin, Biochemistry 46, 9301-9309.
    • (2007) Biochemistry , vol.46 , pp. 9301-9309
    • Rosell, F.I.1    Mauk, M.R.2    Mauk, A.G.3
  • 22
    • 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
  • 23
    • 0029991878 scopus 로고    scopus 로고
    • Hyaluronan-binding properties of human serum hemopexin
    • Hrkal, Z., Kuzelova, K., Müller-Eberhard, U., and Stern, R. (1996) Hyaluronan-binding properties of human serum hemopexin, FEBS Lett. 383, 72-74.
    • (1996) FEBS Lett , vol.383 , pp. 72-74
    • Hrkal, Z.1    Kuzelova, K.2    Müller-Eberhard, U.3    Stern, R.4
  • 25
    • 0015335301 scopus 로고
    • Hemopexin of human and rabbit: Molecular weight and extinction coefficient
    • Seery, V. L., Hathaway, G., and Eberhard, U. M. (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    Eberhard, U.M.3
  • 26
    • 0018167853 scopus 로고
    • Spin states of heme proteins by magnetic circular dichroism
    • Vickery, L. E. (1978) Spin states of heme proteins by magnetic circular dichroism, Methods Enzymol. 54, 284-302.
    • (1978) Methods Enzymol , vol.54 , pp. 284-302
    • Vickery, L.E.1
  • 27
    • 0021798004 scopus 로고
    • The electron paramagnetic resonance of metalloproteins
    • Palmer, G. (1985) The electron paramagnetic resonance of metalloproteins, Biochem. Soc. Trans. 13, 548-560.
    • (1985) Biochem. Soc. Trans , vol.13 , pp. 548-560
    • Palmer, G.1
  • 28
    • 0001731004 scopus 로고
    • Assignment of the axial ligands of ferric ion in low-spin hemoproteins by near-infrared magnetic circular dichroism and electron paramagnetic resonance spectroscopy
    • Gadsby, P. M. A., and Thomson, A. J. (1990) Assignment of the axial ligands of ferric ion in low-spin hemoproteins by near-infrared magnetic circular dichroism and electron paramagnetic resonance spectroscopy, J. Am. Chem. Soc. 112, 5003-5011.
    • (1990) J. Am. Chem. Soc , vol.112 , pp. 5003-5011
    • Gadsby, P.M.A.1    Thomson, A.J.2
  • 29
    • 0033464509 scopus 로고    scopus 로고
    • Magnetic spectroscopic (EPR, ESEEM, Mössbauer, MCD and NMR) studies of low-spin ferriheme centers and their corresponding heme proteins
    • Walker, F. A. (1999) Magnetic spectroscopic (EPR, ESEEM, Mössbauer, MCD and NMR) studies of low-spin ferriheme centers and their corresponding heme proteins, Coord. Chem. Rev. 185-186, 471-534.
    • (1999) Coord. Chem. Rev , vol.185-186 , pp. 471-534
    • Walker, F.A.1
  • 30
    • 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
  • 31
    • 0026071781 scopus 로고
    • Metal-affinity separations: A new dimension in protein processing
    • Arnold, F. H. (1991) Metal-affinity separations: A new dimension in protein processing, Bio/Technology 9, 151-156.
    • (1991) Bio/Technology , vol.9 , pp. 151-156
    • Arnold, F.H.1
  • 32
    • 0024671191 scopus 로고
    • The saga of IMAC and MIT
    • Sulkowski, E. (1989) The saga of IMAC and MIT, Bioessays 10, 170-175.
    • (1989) Bioessays , vol.10 , pp. 170-175
    • Sulkowski, E.1
  • 33
    • 0028076019 scopus 로고
    • Conformational analysis of hemopexin by Fourier-transform infrared and circular dichroism spectroscopy
    • Wu, M. L., and Morgan, W. T. (1994) Conformational analysis of hemopexin by Fourier-transform infrared and circular dichroism spectroscopy, Proteins 20, 185-190.
    • (1994) Proteins , vol.20 , pp. 185-190
    • Wu, M.L.1    Morgan, W.T.2
  • 34
    • 0016374664 scopus 로고
    • Modification of tryptophan residues of rabbit hemopexin by N-bromosuccinimide
    • Morgan, W. T., and Muller-Eberhard, U. (1974) Modification of tryptophan residues of rabbit hemopexin by N-bromosuccinimide, Enzyme 17, 108-115.
    • (1974) Enzyme , vol.17 , pp. 108-115
    • Morgan, W.T.1    Muller-Eberhard, U.2
  • 35
    • 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
  • 36
    • 0028102759 scopus 로고
    • Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins
    • Woody, R. W. (1994) Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins, Eur. Biophys. J. 23, 253-262.
    • (1994) Eur. Biophys. J , vol.23 , pp. 253-262
    • Woody, R.W.1
  • 37
    • 0014703185 scopus 로고
    • 2). 2. Revised heme extinction coefficients and minimal molecular weight
    • 2). 2. Revised heme extinction coefficients and minimal molecular weight, Eur. J. Biochem. 12, 158-164.
    • (1970) Eur. J. Biochem , vol.12 , pp. 158-164
    • Pajot, P.1    Groudinsky, O.2
  • 39
    • 0021211217 scopus 로고
    • Domain structure of rabbit hemopexin. Isolation and characterization of a heme-binding glycopeptide
    • Morgan, W. T., and Smith, A. (1984) Domain structure of rabbit hemopexin. Isolation and characterization of a heme-binding glycopeptide, J. Biol. Chem. 259, 12001-12006.
    • (1984) J. Biol. Chem , vol.259 , pp. 12001-12006
    • Morgan, W.T.1    Smith, A.2
  • 40
  • 41
    • 0017312344 scopus 로고
    • Magnetic circular dichroism studies of myoglobin complexes. Correlations with heme spin state and axial ligation
    • Vickery, L., Nozawa, T., and Sauer, K. (1976) Magnetic circular dichroism studies of myoglobin complexes. Correlations with heme spin state and axial ligation, J. Am. Chem. Soc. 98, 343-350.
    • (1976) J. Am. Chem. Soc , vol.98 , pp. 343-350
    • Vickery, L.1    Nozawa, T.2    Sauer, K.3
  • 42
    • 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
  • 44
    • 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
  • 45
    • 0016272915 scopus 로고
    • Heme complexes of rabbit hemopexin, human hemopexin and human serum albumin: Electron spin resonance and Mössbauer spectroscopic studies
    • Bearden, A. J., Morgan, W. T., and Muller-Eberhard, U. (1974) Heme complexes of rabbit hemopexin, human hemopexin and human serum albumin: Electron spin resonance and Mössbauer spectroscopic studies, Biochem. Biophys. Res. Commun. 61, 265-272.
    • (1974) Biochem. Biophys. Res. Commun , vol.61 , pp. 265-272
    • Bearden, A.J.1    Morgan, W.T.2    Muller-Eberhard, U.3
  • 46
    • 33845279081 scopus 로고    scopus 로고
    • Soltis, S. M., and Strouse, C. E. (1988) Electronic structure of low-spin ferric porphyrins: Single crystal EPR evidence for pseudo-Jahn-Teller distortion in (tetraphenylporphinato)iron(III) bis(imidazole) cations, J. Am. Chem. Soc. 110, 2824-2829.
    • Soltis, S. M., and Strouse, C. E. (1988) Electronic structure of low-spin ferric porphyrins: Single crystal EPR evidence for pseudo-Jahn-Teller distortion in (tetraphenylporphinato)iron(III) bis(imidazole) cations, J. Am. Chem. Soc. 110, 2824-2829.
  • 47
    • 1542334744 scopus 로고    scopus 로고
    • Models of the bis-histidine-ligated electron-transferring cytochromes. Comparative geometric and electronic structure of low-spin ferro- and ferrihemes
    • Walker, F. A. (2004) Models of the bis-histidine-ligated electron-transferring cytochromes. Comparative geometric and electronic structure of low-spin ferro- and ferrihemes, Chem. Rev. 104, 589-615.
    • (2004) Chem. Rev , vol.104 , pp. 589-615
    • Walker, F.A.1
  • 48
    • 0018346044 scopus 로고
    • Induction of hypozincemia and hepatic metallothionein synthesis in hypersensitivity reactions
    • Sobocinski, P. Z., Canterbury, W. J., Jr., Hauer, E. C., and Beall, F. A. (1979) Induction of hypozincemia and hepatic metallothionein synthesis in hypersensitivity reactions, Proc. Soc. Exp. Biol. Med. 160, 175-179.
    • (1979) Proc. Soc. Exp. Biol. Med , vol.160 , pp. 175-179
    • Sobocinski, P.Z.1    Canterbury Jr., W.J.2    Hauer, E.C.3    Beall, F.A.4
  • 49
    • 0020000298 scopus 로고
    • The phenomenon of the acute phase response
    • Kushner, I. (1982) The phenomenon of the acute phase response, Ann. N. Y. Acad. Sci. 389, 39-48.
    • (1982) Ann. N. Y. Acad. Sci , vol.389 , pp. 39-48
    • Kushner, I.1
  • 50
    • 0020609438 scopus 로고
    • Copper metabolism during acute inflammation: Studies on liver and serum copper concentrations in normal and inflamed rats
    • Conforti, A., Franco, L., Milanino, R., Totorizzo, A., and Velo, G. P. (1983) Copper metabolism during acute inflammation: Studies on liver and serum copper concentrations in normal and inflamed rats, Br. J. Pharmacol. 79, 45-52.
    • (1983) Br. J. Pharmacol , vol.79 , pp. 45-52
    • Conforti, A.1    Franco, L.2    Milanino, R.3    Totorizzo, A.4    Velo, G.P.5
  • 51
    • 0023301358 scopus 로고
    • Effect of chronic inflammation on copper and zinc metabolism
    • Oliva, J. C., Castell, M., Queralt, J., and Castellote, C. (1987) Effect of chronic inflammation on copper and zinc metabolism, Rev. Esp. Fisiol. 43, 25-31.
    • (1987) Rev. Esp. Fisiol , vol.43 , pp. 25-31
    • Oliva, J.C.1    Castell, M.2    Queralt, J.3    Castellote, C.4
  • 52
    • 34248165082 scopus 로고    scopus 로고
    • Effect of zinc, copper, and calcium on the structure and stability of serum amyloid A
    • Wang, L., and Colon, W. (2007) Effect of zinc, copper, and calcium on the structure and stability of serum amyloid A, Biochemistry 46, 5562-5569.
    • (2007) Biochemistry , vol.46 , pp. 5562-5569
    • Wang, L.1    Colon, W.2
  • 53
    • 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
  • 54
    • 0003670373 scopus 로고
    • Circular dichroism probes of hemoglobin structure
    • Caughey, W. S, Ed, pp, Academic Press, New York
    • Woody, R. (1978) Circular dichroism probes of hemoglobin structure, in Biochemical and Clinical Aspects of Hemoglobin Abnormalities (Caughey, W. S., Ed.) pp 279-298, Academic Press, New York.
    • (1978) Biochemical and Clinical Aspects of Hemoglobin Abnormalities , pp. 279-298
    • Woody, R.1
  • 55
    • 0018111436 scopus 로고
    • Circular dichroism spectroscopy of hemoproteins
    • Myer, Y. P. (1978) Circular dichroism spectroscopy of hemoproteins, Methods Enzymol. 54, 249-284.
    • (1978) Methods Enzymol , vol.54 , pp. 249-284
    • Myer, Y.P.1
  • 56
    • 0015223110 scopus 로고
    • The origin of the heme Cotton effects in myoglobin and hemoglobin
    • Hsu, M. C., and Woody, R. W. (1971) The origin of the heme Cotton effects in myoglobin and hemoglobin, J. Am. Chem. Soc. 93, 3515-3525.
    • (1971) J. Am. Chem. Soc , vol.93 , pp. 3515-3525
    • Hsu, M.C.1    Woody, R.W.2
  • 57
    • 0000693098 scopus 로고
    • Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins
    • La Mar, G. N., Budd, D. L., Viscio, D. B., Smith, K. M., and Langry, K. C. (1978) Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins, Proc. Natl. Acad. Sci. U.S.A. 75, 5755-5759.
    • (1978) Proc. Natl. Acad. Sci. U.S.A , vol.75 , pp. 5755-5759
    • La Mar, G.N.1    Budd, D.L.2    Viscio, D.B.3    Smith, K.M.4    Langry, K.C.5
  • 59
    • 0022492835 scopus 로고
    • Characterization of haem disorder by circular dichroism
    • Aojula, H. S., Wilson, M. T., and Drake, A. (1986) Characterization of haem disorder by circular dichroism, Biochem. J. 237, 613-616.
    • (1986) Biochem. J , vol.237 , pp. 613-616
    • Aojula, H.S.1    Wilson, M.T.2    Drake, A.3
  • 60
    • 0023819744 scopus 로고
    • 1H-NMR and CD studies of haem orientational disorder in sperm-whale myoglobin and human haemoglobin
    • 1H-NMR and CD studies of haem orientational disorder in sperm-whale myoglobin and human haemoglobin, Biochem. J. 250, 853-858.
    • (1988) Biochem. J , vol.250 , pp. 853-858
    • Aojula, H.S.1    Wilson, M.T.2    Moore, G.R.3    Williamson, D.J.4
  • 62
    • 0021989672 scopus 로고
    • Complete amino acid sequence of human hemopexin, the heme-binding protein of serum
    • Takahashi, N., Takahashi, Y., and Putnam, F. W. (1985) Complete amino acid sequence of human hemopexin, the heme-binding protein of serum, Proc. Natl. Acad. Sci. U.S.A. 82, 72-77.
    • (1985) Proc. Natl. Acad. Sci. U.S.A , vol.82 , pp. 72-77
    • Takahashi, N.1    Takahashi, Y.2    Putnam, F.W.3
  • 63
    • 0027456339 scopus 로고
    • Identification of the histidine residues of hemopexin that coordinate with heme-iron and of a receptor-binding region
    • Morgan, W. T., Muster, P., Tatum, F., Kao, S. M., Alam, J., and Smith, A. (1993) Identification of the histidine residues of hemopexin that coordinate with heme-iron and of a receptor-binding region, J. Biol. Chem. 268, 6256-6262.
    • (1993) J. Biol. Chem , vol.268 , pp. 6256-6262
    • Morgan, W.T.1    Muster, P.2    Tatum, F.3    Kao, S.M.4    Alam, J.5    Smith, A.6
  • 64
    • 0026035512 scopus 로고
    • Rat hemopexin. Molecular cloning, primary structural characterization, and analysis of gene expression
    • Nikkila, H., Gitlin, J. D., and Müller-Eberhard, U. (1991) Rat hemopexin. Molecular cloning, primary structural characterization, and analysis of gene expression, Biochemistry 30, 823-829.
    • (1991) Biochemistry , vol.30 , pp. 823-829
    • Nikkila, H.1    Gitlin, J.D.2    Müller-Eberhard, U.3
  • 65
    • 33646200456 scopus 로고    scopus 로고
    • Investigating the local flexibility of functional residues in hemoproteins
    • Sacquin-Mora, S., and Lavery, R. (2006) Investigating the local flexibility of functional residues in hemoproteins, Biophys. J. 90, 2706-2717.
    • (2006) Biophys. J , vol.90 , pp. 2706-2717
    • Sacquin-Mora, S.1    Lavery, R.2
  • 66
    • 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
  • 67
    • 0023100151 scopus 로고
    • Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins
    • Aojula, H. S., Wilson, M. T., and Morrison, I. G. (1987) Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins, Biochem. J. 243, 205-210.
    • (1987) Biochem. J , vol.243 , pp. 205-210
    • Aojula, H.S.1    Wilson, M.T.2    Morrison, I.G.3
  • 68
    • 0023108441 scopus 로고
    • Functional effects of heme orientational disorder in sperm whale myoglobin
    • Light, W. R., Rohlfs, R. J., Palmer, G., and Olson, J. S. (1987) Functional effects of heme orientational disorder in sperm whale myoglobin, J. Biol. Chem. 262, 46-52.
    • (1987) J. Biol. Chem , vol.262 , pp. 46-52
    • Light, W.R.1    Rohlfs, R.J.2    Palmer, G.3    Olson, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.