메뉴 건너뛰기




Volumn 369, Issue 1, 2007, Pages 87-104

Use of stable isotopically enriched proteins and directly coupled high-performance liquid chromatography inductively coupled plasma mass spectrometry for quantitatively monitoring the transfer of metals between proteins

Author keywords

67Zn; Carbonic anhydrase; Directly coupled HPLC ICP MS; Metallothionein

Indexed keywords

CARBONIC ANHYDRASE; CHEMICAL ACTIVATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; INDUCTIVELY COUPLED PLASMA; INDUCTIVELY COUPLED PLASMA MASS SPECTROMETRY; ION EXCHANGE; MOLAR RATIO; PEPTIDES; ZINC;

EID: 34548283175     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2007.06.015     Document Type: Article
Times cited : (13)

References (81)
  • 1
    • 0032584166 scopus 로고    scopus 로고
    • Thiolate ligands in metallothionein confer redox activity on zinc clusters
    • Maret W., and Vallee B.L. Thiolate ligands in metallothionein confer redox activity on zinc clusters. Proc. Natl. Acad. Sci. USA 95 (1998) 3478-3482
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3478-3482
    • Maret, W.1    Vallee, B.L.2
  • 2
    • 1542364374 scopus 로고    scopus 로고
    • Metallothioneins: zinc, cadmium, mercury, and copper thiolates and selenolates mimicking protein active site features: structural aspects and biological implications
    • Henkel G., and Krebs B. Metallothioneins: zinc, cadmium, mercury, and copper thiolates and selenolates mimicking protein active site features: structural aspects and biological implications. Chem. Rev. 104 (2004) 801-824
    • (2004) Chem. Rev. , vol.104 , pp. 801-824
    • Henkel, G.1    Krebs, B.2
  • 4
    • 0031818254 scopus 로고    scopus 로고
    • Expression of the gene encoding metallothionein-3 in organs of the reproductive system
    • Moffat P., and Sequin C. Expression of the gene encoding metallothionein-3 in organs of the reproductive system. DNA Cell Biol. 17 (1998) 501-510
    • (1998) DNA Cell Biol. , vol.17 , pp. 501-510
    • Moffat, P.1    Sequin, C.2
  • 6
    • 0030052798 scopus 로고    scopus 로고
    • Activation of the complete mouse metallothionein gene locus in the maternal deciduum
    • Liang L., Fu K., Lee D.K., Sobieski R.J., Dalton T., and Andrews G.K. Activation of the complete mouse metallothionein gene locus in the maternal deciduum. Mol. Reprod. Dev. 43 (1996) 25-37
    • (1996) Mol. Reprod. Dev. , vol.43 , pp. 25-37
    • Liang, L.1    Fu, K.2    Lee, D.K.3    Sobieski, R.J.4    Dalton, T.5    Andrews, G.K.6
  • 7
    • 0021944046 scopus 로고
    • Possible role for metallothionein in protection against radiation-induced oxidative stress: kinetics and mechanism of its reaction with superoxide and hydroxyl radicals
    • Thornalley P.J., and Vǎsak M. Possible role for metallothionein in protection against radiation-induced oxidative stress: kinetics and mechanism of its reaction with superoxide and hydroxyl radicals. Biochim. Biophys. Acta 827 (1985) 36-44
    • (1985) Biochim. Biophys. Acta , vol.827 , pp. 36-44
    • Thornalley, P.J.1    Vǎsak, M.2
  • 8
    • 0023755124 scopus 로고
    • Tissue-specific regulation of zinc metabolism and metallothionein genes by interleukin 1
    • Cousins R.J., and Leinart A.S. Tissue-specific regulation of zinc metabolism and metallothionein genes by interleukin 1. FASEB J. 13 (1988) 2884-2890
    • (1988) FASEB J. , vol.13 , pp. 2884-2890
    • Cousins, R.J.1    Leinart, A.S.2
  • 9
    • 0032192504 scopus 로고    scopus 로고
    • Localization of metallothionein-I and -III expression in the CNS of transgenic mice with astrocyte-targeted expression of interleukin 6
    • Carrasco J., Hernández J., González B., Campbell I., and Hidalgo J. Localization of metallothionein-I and -III expression in the CNS of transgenic mice with astrocyte-targeted expression of interleukin 6. Exp. Neurol. 153 (1998) 184-194
    • (1998) Exp. Neurol. , vol.153 , pp. 184-194
    • Carrasco, J.1    Hernández, J.2    González, B.3    Campbell, I.4    Hidalgo, J.5
  • 10
    • 0027973612 scopus 로고
    • Establishment of the role of IL-6 and TNF receptor 1 using gene knockout mice
    • Bluethmann H., Rothe J., Schultze N., Tkachuk M., and Koebel P. Establishment of the role of IL-6 and TNF receptor 1 using gene knockout mice. J. Leukocyte Biol. 56 (1994) 565-570
    • (1994) J. Leukocyte Biol. , vol.56 , pp. 565-570
    • Bluethmann, H.1    Rothe, J.2    Schultze, N.3    Tkachuk, M.4    Koebel, P.5
  • 11
    • 0033990794 scopus 로고    scopus 로고
    • Regulation of metallothionein gene expression by oxidative stress and metal ions
    • Andrews G.K. Regulation of metallothionein gene expression by oxidative stress and metal ions. Biochem. Pharmacol. 59 (2000) 95-104
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 95-104
    • Andrews, G.K.1
  • 12
    • 33749641286 scopus 로고    scopus 로고
    • Metallothionein redox cycle and function
    • Kang Y.J. Metallothionein redox cycle and function. Exp. Biol. Med. 231 (2006) 1459-1467
    • (2006) Exp. Biol. Med. , vol.231 , pp. 1459-1467
    • Kang, Y.J.1
  • 13
    • 0000119940 scopus 로고
    • Structure of the metal clusters in rabbit liver metallothionein
    • Otvos J.D., and Armitage I.M. Structure of the metal clusters in rabbit liver metallothionein. Proc. Natl. Acad. Sci. USA 77 (1980) 7094-7098
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7094-7098
    • Otvos, J.D.1    Armitage, I.M.2
  • 14
    • 0021829810 scopus 로고
    • Distinct metal-binding configurations in metallothionein
    • Neilson K.B., Atkin C.L., and Winge D.R. Distinct metal-binding configurations in metallothionein. J. Biol. Chem. 260 (1985) 5342-5350
    • (1985) J. Biol. Chem. , vol.260 , pp. 5342-5350
    • Neilson, K.B.1    Atkin, C.L.2    Winge, D.R.3
  • 15
    • 0004205702 scopus 로고
    • Dynamic aspects of metallothionein structure
    • Suzuki K.T., Imura N., and Kimura M. (Eds), Birkhäuser Verlag, Basel, Switzerland
    • Otvos J.D., Liu X., Li H., Shen G., and Basti M. Dynamic aspects of metallothionein structure. In: Suzuki K.T., Imura N., and Kimura M. (Eds). Metallothionein III (1993), Birkhäuser Verlag, Basel, Switzerland 57-74
    • (1993) Metallothionein III , pp. 57-74
    • Otvos, J.D.1    Liu, X.2    Li, H.3    Shen, G.4    Basti, M.5
  • 16
    • 0022429040 scopus 로고
    • 113Cd NMR studies of homogeneous reconstituted metallothionein: reaffirmation of the two-cluster arrangement of metals
    • 113Cd NMR studies of homogeneous reconstituted metallothionein: reaffirmation of the two-cluster arrangement of metals. Biochemistry 24 (1985) 6735-6740
    • (1985) Biochemistry , vol.24 , pp. 6735-6740
    • Otvos, J.D.1    Engeseth, H.R.2    Wehrli, S.3
  • 17
    • 0021356888 scopus 로고
    • Preferential binding of copper to the β domain of metallothionein
    • Nielson K.B., and Winge D.R. Preferential binding of copper to the β domain of metallothionein. J. Biol. Chem. 259 (1984) 4941-4946
    • (1984) J. Biol. Chem. , vol.259 , pp. 4941-4946
    • Nielson, K.B.1    Winge, D.R.2
  • 18
    • 0022482177 scopus 로고
    • Structural study of the copper and zinc sites in metallothioneins by using extended X-ray absorption fine structure
    • Abrahams I.L., Bremner I., Diakun G.P., Garner C.D., Hasnain S.S., Ross I., and Vasák M. Structural study of the copper and zinc sites in metallothioneins by using extended X-ray absorption fine structure. Biochem. J. 236 (1986) 585-589
    • (1986) Biochem. J. , vol.236 , pp. 585-589
    • Abrahams, I.L.1    Bremner, I.2    Diakun, G.P.3    Garner, C.D.4    Hasnain, S.S.5    Ross, I.6    Vasák, M.7
  • 19
    • 0023098760 scopus 로고
    • Involvement of metallothionein in the hepatic metabolism of copper
    • Bremner I. Involvement of metallothionein in the hepatic metabolism of copper. Am. Inst. Nutr. 117 (1987) 19-29
    • (1987) Am. Inst. Nutr. , vol.117 , pp. 19-29
    • Bremner, I.1
  • 20
    • 0022610911 scopus 로고
    • Quantification of metallothioneins by a silver saturation method
    • Scheuhammer A.M., and Cherian M.G. Quantification of metallothioneins by a silver saturation method. Toxicol. Appl. Pharmacol. 82 (1986) 417-425
    • (1986) Toxicol. Appl. Pharmacol. , vol.82 , pp. 417-425
    • Scheuhammer, A.M.1    Cherian, M.G.2
  • 21
  • 22
    • 0026448118 scopus 로고
    • Zinc rapidly induces a metal response element-binding factor
    • Czupryn M., Brown W.E., and Vallee B.L. Zinc rapidly induces a metal response element-binding factor. Proc. Natl. Acad. Sci. USA 89 (1992) 10395-10399
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10395-10399
    • Czupryn, M.1    Brown, W.E.2    Vallee, B.L.3
  • 23
    • 0032967906 scopus 로고    scopus 로고
    • Differential metal response and regulation of human heavy metal-inducible genes
    • Murata M., Gong P., Suzuki K., and Koizumi S. Differential metal response and regulation of human heavy metal-inducible genes. J. Cell. Physiol. 180 (1999) 105-113
    • (1999) J. Cell. Physiol. , vol.180 , pp. 105-113
    • Murata, M.1    Gong, P.2    Suzuki, K.3    Koizumi, S.4
  • 24
    • 0030909001 scopus 로고    scopus 로고
    • Reversible activation of mouse metal response element-binding transcription factor 1 DNA binding involves zinc interaction with the zinc finger domain
    • Dalton T.P., Bittel D., and Andrews G.K. Reversible activation of mouse metal response element-binding transcription factor 1 DNA binding involves zinc interaction with the zinc finger domain. Mol. Cell. Biol. 17 (1997) 2781-2789
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2781-2789
    • Dalton, T.P.1    Bittel, D.2    Andrews, G.K.3
  • 25
    • 0025785257 scopus 로고
    • Intracellular free zinc and zinc buffering in human red blood cells
    • Simons T.J.B. Intracellular free zinc and zinc buffering in human red blood cells. J. Membr. Biol. 123 (1991) 63-71
    • (1991) J. Membr. Biol. , vol.123 , pp. 63-71
    • Simons, T.J.B.1
  • 26
    • 0032584091 scopus 로고    scopus 로고
    • Recent excitement regarding metallothionein
    • Fischer E.H., and Davie E.W. Recent excitement regarding metallothionein. Proc. Natl. Acad. Sci. USA 95 (1998) 3333-3334
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3333-3334
    • Fischer, E.H.1    Davie, E.W.2
  • 27
    • 0033514994 scopus 로고    scopus 로고
    • Inhibition sites in enzymes: zinc removal and reactivation by thionein
    • Maret W., Jacob C., Vallee B.L., and Fischer E.H. Inhibition sites in enzymes: zinc removal and reactivation by thionein. Proc. Natl. Acad. Sci. USA 96 (1999) 1936-1940
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1936-1940
    • Maret, W.1    Jacob, C.2    Vallee, B.L.3    Fischer, E.H.4
  • 28
    • 1642389890 scopus 로고    scopus 로고
    • Zinc and sulfur: a critical biochemical partnership
    • Maret W. Zinc and sulfur: a critical biochemical partnership. Biochemistry 43 (2004) 3301-3309
    • (2004) Biochemistry , vol.43 , pp. 3301-3309
    • Maret, W.1
  • 29
    • 33749034376 scopus 로고
    • Structure-reactivity relationships of metallothionein, a unique metal-binding protein
    • Otvos J.D., Petering D.H., and Shaw C.F. Structure-reactivity relationships of metallothionein, a unique metal-binding protein. Comments Inorg. Chem. 9 (1989) 1-35
    • (1989) Comments Inorg. Chem. , vol.9 , pp. 1-35
    • Otvos, J.D.1    Petering, D.H.2    Shaw, C.F.3
  • 30
    • 0025719287 scopus 로고
    • Zinc transfer from transcription factor IIA fingers to thionein clusters
    • Zeng J., Vallee B.L., and Kägi J.H.R. Zinc transfer from transcription factor IIA fingers to thionein clusters. Proc. Natl. Acad. Sci. USA 88 (1991) 9984-9988
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9984-9988
    • Zeng, J.1    Vallee, B.L.2    Kägi, J.H.R.3
  • 31
    • 0032504163 scopus 로고    scopus 로고
    • Modulation of DNA binding of a tramtrack zinc finger peptide by the metallothionein-thionein conjugate pair
    • Roesijadi G., Bogumil R., Vasak M., and Kägi H.R. Modulation of DNA binding of a tramtrack zinc finger peptide by the metallothionein-thionein conjugate pair. J. Biol. Chem. 273 (1998) 17425-17432
    • (1998) J. Biol. Chem. , vol.273 , pp. 17425-17432
    • Roesijadi, G.1    Bogumil, R.2    Vasak, M.3    Kägi, H.R.4
  • 32
    • 0031766835 scopus 로고    scopus 로고
    • Monitoring metal ion flux in reactions of metallothionein and drug-modified metallothionein by electrospray mass spectrometry
    • Zaia J., Fabris D., Wei D., Karpel R.L., and Feneslau C. Monitoring metal ion flux in reactions of metallothionein and drug-modified metallothionein by electrospray mass spectrometry. Protein Sci. 7 (1998) 2398-2404
    • (1998) Protein Sci. , vol.7 , pp. 2398-2404
    • Zaia, J.1    Fabris, D.2    Wei, D.3    Karpel, R.L.4    Feneslau, C.5
  • 33
    • 0028082427 scopus 로고
    • Oxidative metal release from metallothionein via zinc-thiol/disulphide exchange
    • Maret W. Oxidative metal release from metallothionein via zinc-thiol/disulphide exchange. Proc. Natl. Acad. Sci. USA 91 (1994) 237-241
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 237-241
    • Maret, W.1
  • 34
    • 0034058549 scopus 로고    scopus 로고
    • The function of zinc metallothionein: a link between cellular zinc and redox state
    • Maret W. The function of zinc metallothionein: a link between cellular zinc and redox state. J. Nutr. 130 (2000) 1455S-1458S
    • (2000) J. Nutr. , vol.130
    • Maret, W.1
  • 35
    • 0032742299 scopus 로고    scopus 로고
    • Metal regulation of metallothionein participation in redox reactions
    • Zhang S., Li J., Wang C.C., and Tsou C.L. Metal regulation of metallothionein participation in redox reactions. FEBS Lett. 462 (1999) 383-386
    • (1999) FEBS Lett. , vol.462 , pp. 383-386
    • Zhang, S.1    Li, J.2    Wang, C.C.3    Tsou, C.L.4
  • 36
    • 0032584186 scopus 로고    scopus 로고
    • Control of zinc transfer between thionein, metallothionein, and zinc proteins
    • Jacob C., Maret W., and Vallee B.L. Control of zinc transfer between thionein, metallothionein, and zinc proteins. Proc. Natl. Acad. Sci. USA 95 (1998) 3489-3494
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3489-3494
    • Jacob, C.1    Maret, W.2    Vallee, B.L.3
  • 38
    • 33644866812 scopus 로고    scopus 로고
    • Metallothionein disulfides are present in metallothionein-overexpressing transgenic mouse heart and increase under conditions of oxidative stress
    • Feng W., Benz F.W., Cai J., Pierce W.M., and Kang Y.J. Metallothionein disulfides are present in metallothionein-overexpressing transgenic mouse heart and increase under conditions of oxidative stress. J. Biol. Chem. 281 (2006) 681-687
    • (2006) J. Biol. Chem. , vol.281 , pp. 681-687
    • Feng, W.1    Benz, F.W.2    Cai, J.3    Pierce, W.M.4    Kang, Y.J.5
  • 39
    • 0019527166 scopus 로고
    • On the reactivity of metallothioneins with 5,5′-dithiobis(2-nitrobenzoic acid)
    • Li T.Y., Minkel D.T., Shaw III C.F., and Petering D.H. On the reactivity of metallothioneins with 5,5′-dithiobis(2-nitrobenzoic acid). Biochem. J. 193 (1981) 441-446
    • (1981) Biochem. J. , vol.193 , pp. 441-446
    • Li, T.Y.1    Minkel, D.T.2    Shaw III, C.F.3    Petering, D.H.4
  • 40
    • 0034785967 scopus 로고    scopus 로고
    • The effects of physiologically important nonmetallic ligands in the reactivity of metallothionein towards 5,5′(-dithiobis(2-nitrobenzoic acid)
    • Kangur L., and Palumaa P. The effects of physiologically important nonmetallic ligands in the reactivity of metallothionein towards 5,5′(-dithiobis(2-nitrobenzoic acid). Eur. J. Biochem. 268 (2001) 4979-4984
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4979-4984
    • Kangur, L.1    Palumaa, P.2
  • 41
    • 0034859512 scopus 로고    scopus 로고
    • Catalytic oxidation of zinc/sulfur coordination sites in proteins by selenium compounds
    • Chen Y., and Maret W. Catalytic oxidation of zinc/sulfur coordination sites in proteins by selenium compounds. Antioxid. Redox Signal. 3 (2001) 651-656
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 651-656
    • Chen, Y.1    Maret, W.2
  • 42
    • 0036312378 scopus 로고    scopus 로고
    • Qualitative characterization of biomolecular zinc complexes by collisionally induced dissociation
    • Afonso C., Hathout Y., and Fenselau C. Qualitative characterization of biomolecular zinc complexes by collisionally induced dissociation. J. Mass Spectrom. 37 (2002) 755-759
    • (2002) J. Mass Spectrom. , vol.37 , pp. 755-759
    • Afonso, C.1    Hathout, Y.2    Fenselau, C.3
  • 43
    • 2942516407 scopus 로고    scopus 로고
    • Metal donation and apo-metalloenzyme activation by stable isotopically labeled metallothionein
    • Mason A.Z., Perico N., Moeller R., Thrippleton K., Potter T., and Lloyd D. Metal donation and apo-metalloenzyme activation by stable isotopically labeled metallothionein. Mar. Environ. Res. 58 (2004) 371-375
    • (2004) Mar. Environ. Res. , vol.58 , pp. 371-375
    • Mason, A.Z.1    Perico, N.2    Moeller, R.3    Thrippleton, K.4    Potter, T.5    Lloyd, D.6
  • 44
    • 0032584078 scopus 로고    scopus 로고
    • The glutathione redox couple modulates zinc transfer from metallothionein to zinc depleted sorbitol dehydrogenase
    • Jiang L.-J., Maret W., and Vallee B.L. The glutathione redox couple modulates zinc transfer from metallothionein to zinc depleted sorbitol dehydrogenase. Proc. Natl. Acad. Sci. USA 95 (1998) 3483-3488
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3483-3488
    • Jiang, L.-J.1    Maret, W.2    Vallee, B.L.3
  • 45
    • 34548282672 scopus 로고    scopus 로고
    • Metalloprotein crosstalk: quantifying Zn atom exchange between isotopically labeled proteins using directly coupled HPLC-ICP-MS
    • Holland G., and Bandura D.R. (Eds), Royal Society of Chemistry, London
    • Mason A.Z., Potter T., Webster J., and Meraz R.F. Metalloprotein crosstalk: quantifying Zn atom exchange between isotopically labeled proteins using directly coupled HPLC-ICP-MS. In: Holland G., and Bandura D.R. (Eds). Plasma Source Mass Spectrometry: Current Trends and Future Developments (2005), Royal Society of Chemistry, London 3-27
    • (2005) Plasma Source Mass Spectrometry: Current Trends and Future Developments , pp. 3-27
    • Mason, A.Z.1    Potter, T.2    Webster, J.3    Meraz, R.F.4
  • 46
    • 0032123423 scopus 로고    scopus 로고
    • Cytosolic metal speciation studies by sequential, on-line, SE-IE/HPLC-ICPMS
    • Mason A.Z., and Meraz R. Cytosolic metal speciation studies by sequential, on-line, SE-IE/HPLC-ICPMS. Mar. Environ. Res. 46 (1998) 573-577
    • (1998) Mar. Environ. Res. , vol.46 , pp. 573-577
    • Mason, A.Z.1    Meraz, R.2
  • 47
    • 0025322373 scopus 로고
    • Metallothionein separation and analysis by directly coupled size exclusion high performance liquid chromatography inductively coupled plasma mass spectroscopy
    • Mason A.Z., Storms S.D., and Jenkins K.D. Metallothionein separation and analysis by directly coupled size exclusion high performance liquid chromatography inductively coupled plasma mass spectroscopy. Anal. Biochem. 186 (1990) 187-201
    • (1990) Anal. Biochem. , vol.186 , pp. 187-201
    • Mason, A.Z.1    Storms, S.D.2    Jenkins, K.D.3
  • 48
    • 0036753396 scopus 로고    scopus 로고
    • A study of Cu turnover in proteins of the visceral complex of Littorina littorea by isotopic ratio analysis using ICP-MS
    • Mason A.Z., and Borja M. A study of Cu turnover in proteins of the visceral complex of Littorina littorea by isotopic ratio analysis using ICP-MS. Mar. Environ. Res. 54 (2002) 351-355
    • (2002) Mar. Environ. Res. , vol.54 , pp. 351-355
    • Mason, A.Z.1    Borja, M.2
  • 49
    • 0026323592 scopus 로고
    • Metal removal from mammalian metallothioneins
    • Hunziker P.E. Metal removal from mammalian metallothioneins. Methods Enzymol. 205 (1991) 451-452
    • (1991) Methods Enzymol. , vol.205 , pp. 451-452
    • Hunziker, P.E.1
  • 50
    • 0026318278 scopus 로고
    • Metal removal and substitution in vertebrate and invertebrate metallothioneins
    • Vǎsak M. Metal removal and substitution in vertebrate and invertebrate metallothioneins. Methods Enzymol. 205 (1991) 453-458
    • (1991) Methods Enzymol. , vol.205 , pp. 453-458
    • Vǎsak, M.1
  • 51
    • 0018551794 scopus 로고
    • Spectroscopic properties of zinc-metallothionein
    • Bu{combining double acute accent}hler R.H., and Kagi J.H. Spectroscopic properties of zinc-metallothionein. Exp. Suppl. 34 (1979) 211-220
    • (1979) Exp. Suppl. , vol.34 , pp. 211-220
    • Buhler, R.H.1    Kagi, J.H.2
  • 52
    • 0017413628 scopus 로고
    • Coordination chemical studies on metalloenzymes: II. Kinetic behavior of various types of chelating agents towards bovine carbonic anhydrase
    • Kidani Y., and Hirose J. Coordination chemical studies on metalloenzymes: II. Kinetic behavior of various types of chelating agents towards bovine carbonic anhydrase. J. Biochem. (Tokyo) 81 (1977) 1383-1391
    • (1977) J. Biochem. (Tokyo) , vol.81 , pp. 1383-1391
    • Kidani, Y.1    Hirose, J.2
  • 53
    • 0017393793 scopus 로고
    • A rapid and convenient preparation of apo-carbonic anhydrase
    • Hunt J.B., Rhee M.J., and Storm C.B. A rapid and convenient preparation of apo-carbonic anhydrase. Anal. Biochem. 79 (1977) 614-617
    • (1977) Anal. Biochem. , vol.79 , pp. 614-617
    • Hunt, J.B.1    Rhee, M.J.2    Storm, C.B.3
  • 54
    • 0020549814 scopus 로고
    • Inactivation of bovine carbonic anhydrase by dipicolinate: kinetic studies and mechanistic implications
    • Pocker Y., and Fong C.T.O. Inactivation of bovine carbonic anhydrase by dipicolinate: kinetic studies and mechanistic implications. Biochemistry 22 (1983) 813-818
    • (1983) Biochemistry , vol.22 , pp. 813-818
    • Pocker, Y.1    Fong, C.T.O.2
  • 55
    • 0142195996 scopus 로고    scopus 로고
    • Characterization of metallothionein isoforms from rabbit liver by liquid chromatography coupled to electrospray mass spectrometry
    • Sanz-Nebot V., Andón B., and Barbosa J. Characterization of metallothionein isoforms from rabbit liver by liquid chromatography coupled to electrospray mass spectrometry. J. Chromatogr. B 796 (2003) 379-393
    • (2003) J. Chromatogr. B , vol.796 , pp. 379-393
    • Sanz-Nebot, V.1    Andón, B.2    Barbosa, J.3
  • 56
    • 0030849266 scopus 로고    scopus 로고
    • Structure and mechanism of carbonic anhydrase
    • Lindskog S. Structure and mechanism of carbonic anhydrase. Pharmacol. Ther. 74 (1997) 1-20
    • (1997) Pharmacol. Ther. , vol.74 , pp. 1-20
    • Lindskog, S.1
  • 57
    • 0019013769 scopus 로고
    • Reactivation in vitro of zinc-requiring apo-enzymes by rat liver zinc-thionein
    • Udom A.O., and Brady F.O. Reactivation in vitro of zinc-requiring apo-enzymes by rat liver zinc-thionein. Biochem. J. 187 (1980) 329-335
    • (1980) Biochem. J. , vol.187 , pp. 329-335
    • Udom, A.O.1    Brady, F.O.2
  • 58
    • 0000191704 scopus 로고
    • Metal binding and catalytic activity in bovine carbonic anhydrase
    • Lindskog S., and Malmström B.G. Metal binding and catalytic activity in bovine carbonic anhydrase. J. Biol. Chem. 237 (1962) 1129-1137
    • (1962) J. Biol. Chem. , vol.237 , pp. 1129-1137
    • Lindskog, S.1    Malmström, B.G.2
  • 59
    • 0035814762 scopus 로고    scopus 로고
    • Stoichiometry in zinc ion transfer from metallothionein to a zinc-finger peptide
    • Hathout Y., Fabris D., and Fenselau C. Stoichiometry in zinc ion transfer from metallothionein to a zinc-finger peptide. Int. J. Mass Spectrom. Ion Proc. 204 (2001) 1-6
    • (2001) Int. J. Mass Spectrom. Ion Proc. , vol.204 , pp. 1-6
    • Hathout, Y.1    Fabris, D.2    Fenselau, C.3
  • 60
    • 0034646226 scopus 로고    scopus 로고
    • Zinc transfer potentials of the α- and β-clusters of metallothionein are affected by domain interactions in the whole molecule
    • Jiang L.-J., Vasák M., Vallee B.L., and Maret M. Zinc transfer potentials of the α- and β-clusters of metallothionein are affected by domain interactions in the whole molecule. Proc. Natl. Acad. Sci. USA 97 (2000) 2503-2508
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2503-2508
    • Jiang, L.-J.1    Vasák, M.2    Vallee, B.L.3    Maret, M.4
  • 61
    • 0035826695 scopus 로고    scopus 로고
    • Differential fluorescence labeling of cysteinyl clusters uncovers high tissue levels of thionein
    • Yang Y., Maret W., and Vallee B.L. Differential fluorescence labeling of cysteinyl clusters uncovers high tissue levels of thionein. Proc. Natl. Acad. Sci. USA 98 (2001) 5556-5559
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5556-5559
    • Yang, Y.1    Maret, W.2    Vallee, B.L.3
  • 62
    • 0027204255 scopus 로고
    • A putative glutathione-binding site in CdZn-metallothionein identified by equilibrium binding and molecular-modelling studies
    • Brouwer M., Hoexum-Brouwer T., and Cashon R.E. A putative glutathione-binding site in CdZn-metallothionein identified by equilibrium binding and molecular-modelling studies. Biochem. J. (1993) 219-225
    • (1993) Biochem. J. , pp. 219-225
    • Brouwer, M.1    Hoexum-Brouwer, T.2    Cashon, R.E.3
  • 63
    • 0024264526 scopus 로고
    • Glutathione metabolism and its selective modification
    • Meister A. Glutathione metabolism and its selective modification. J. Biol. Chem. 263 (1988) 17205-17208
    • (1988) J. Biol. Chem. , vol.263 , pp. 17205-17208
    • Meister, A.1
  • 65
    • 0023803036 scopus 로고
    • Kinetic lability of zinc bound to metallothionein in Ehrlich cells
    • Krezoski S.K., Villalobos J., Shaw III C.F., and Petering D.H. Kinetic lability of zinc bound to metallothionein in Ehrlich cells. Biochem. J. 255 (1988) 483-491
    • (1988) Biochem. J. , vol.255 , pp. 483-491
    • Krezoski, S.K.1    Villalobos, J.2    Shaw III, C.F.3    Petering, D.H.4
  • 66
    • 0037081472 scopus 로고    scopus 로고
    • Dynamics of interdomain and intermolecular interactions in mammalian metallothioneins
    • Zangger K., and Armitage I.M. Dynamics of interdomain and intermolecular interactions in mammalian metallothioneins. J. Inorg. Biochem. 88 (2002) 135-143
    • (2002) J. Inorg. Biochem. , vol.88 , pp. 135-143
    • Zangger, K.1    Armitage, I.M.2
  • 67
    • 0022397076 scopus 로고
    • Products of metal exchange reactions in metallothionein
    • Nettesheim D.G., Engeseth H.R., and Otvos J.D. Products of metal exchange reactions in metallothionein. Biochemistry 24 (1985) 6744-6751
    • (1985) Biochemistry , vol.24 , pp. 6744-6751
    • Nettesheim, D.G.1    Engeseth, H.R.2    Otvos, J.D.3
  • 68
    • 0030033203 scopus 로고    scopus 로고
    • Evidence that nitric oxide enhances cadmium toxicity by displacing cadmium from metallothionein
    • Misra R.R., Hochadel J.F., Smith G.T., Cook J.C., and Waalkes M.P. Evidence that nitric oxide enhances cadmium toxicity by displacing cadmium from metallothionein. Chem. Res. Toxicol. 9 (1996) 326-332
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 326-332
    • Misra, R.R.1    Hochadel, J.F.2    Smith, G.T.3    Cook, J.C.4    Waalkes, M.P.5
  • 69
    • 0023609534 scopus 로고
    • Glutathione, a first line of defense against cadmium toxicity
    • Singhal R.K., Anderson M.E., and Meister A. Glutathione, a first line of defense against cadmium toxicity. FASEB J. 3 (1987) 220-223
    • (1987) FASEB J. , vol.3 , pp. 220-223
    • Singhal, R.K.1    Anderson, M.E.2    Meister, A.3
  • 70
    • 0024554012 scopus 로고
    • The role of glutathione in copper metabolism and toxicity
    • Freedman J.H., Ciriolo M.R., and Peisach J. The role of glutathione in copper metabolism and toxicity. J. Biol. Chem. 264 (1989) 5598-5605
    • (1989) J. Biol. Chem. , vol.264 , pp. 5598-5605
    • Freedman, J.H.1    Ciriolo, M.R.2    Peisach, J.3
  • 71
    • 0027204069 scopus 로고
    • Targeting and germ-line transmission of a null mutation at the metallothionein I and II loci in mouse
    • Michalska A.E., and Choo K.H. Targeting and germ-line transmission of a null mutation at the metallothionein I and II loci in mouse. Proc. Natl. Acad. Sci. USA 90 (1993) 8088-8092
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8088-8092
    • Michalska, A.E.1    Choo, K.H.2
  • 73
    • 0032555204 scopus 로고    scopus 로고
    • The elusive function of metallothioneins
    • Palmiter R.D. The elusive function of metallothioneins. Proc. Natl. Acad. Sci. USA 95 (1998) 8428-8430
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8428-8430
    • Palmiter, R.D.1
  • 74
    • 0034209333 scopus 로고    scopus 로고
    • Detection and identification of rabbit liver metallothionein-2 subisoforms by capillary zone electrophoresis-inductively coupled plasma mass spectrometry and microbore HPLC-electrospray mass spectrometry
    • Chassaigne H., Mounicou S., Casiot C., Lobinski R., and Potin-Gautier M. Detection and identification of rabbit liver metallothionein-2 subisoforms by capillary zone electrophoresis-inductively coupled plasma mass spectrometry and microbore HPLC-electrospray mass spectrometry. Analysis 28 (2000) 357-360
    • (2000) Analysis , vol.28 , pp. 357-360
    • Chassaigne, H.1    Mounicou, S.2    Casiot, C.3    Lobinski, R.4    Potin-Gautier, M.5
  • 75
    • 27744516641 scopus 로고    scopus 로고
    • Elemental speciation analysis by capillary electrophoresis with ICP-MS and electrospray mass spectrometric detection
    • Lobinski R. Elemental speciation analysis by capillary electrophoresis with ICP-MS and electrospray mass spectrometric detection. Anal. Sci. 17 (2001) 41-43
    • (2001) Anal. Sci. , vol.17 , pp. 41-43
    • Lobinski, R.1
  • 76
    • 0346024186 scopus 로고    scopus 로고
    • Identification of a metallothionein in Synechococcus by capillary electrophoresis hyphenated with inductively coupled plasma mass spectrometry
    • Lavorante A.F., Gine M.F., Gervasio A.P., Miranda C.E., Fiore M.F., Bellato C.M., and Carrilho E. Identification of a metallothionein in Synechococcus by capillary electrophoresis hyphenated with inductively coupled plasma mass spectrometry. Anal. Sci. 19 (2003) 1611-1616
    • (2003) Anal. Sci. , vol.19 , pp. 1611-1616
    • Lavorante, A.F.1    Gine, M.F.2    Gervasio, A.P.3    Miranda, C.E.4    Fiore, M.F.5    Bellato, C.M.6    Carrilho, E.7
  • 77
    • 0022006840 scopus 로고
    • Isolation and characterization of six human hepatic isometallothioneins
    • Hunziker P.E., and Kagi H.R. Isolation and characterization of six human hepatic isometallothioneins. Biochem. J. 231 (1985) 375-382
    • (1985) Biochem. J. , vol.231 , pp. 375-382
    • Hunziker, P.E.1    Kagi, H.R.2
  • 78
    • 0033995621 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry of zinc, cadmium, and copper metallothioneins: evidence for metal-binding cooperativity
    • Gehrig P.M., You C., Dallinger R., Gruber C., Brouwer M., Kagi J.H., and Hunziker P.E. Electrospray ionization mass spectrometry of zinc, cadmium, and copper metallothioneins: evidence for metal-binding cooperativity. Protein Sci. 9 (2000) 395-402
    • (2000) Protein Sci. , vol.9 , pp. 395-402
    • Gehrig, P.M.1    You, C.2    Dallinger, R.3    Gruber, C.4    Brouwer, M.5    Kagi, J.H.6    Hunziker, P.E.7
  • 80
    • 33645454832 scopus 로고    scopus 로고
    • 68Zn isotope exchange experiments reveal an unusual kinetic lability of the metal ions in the di-zinc form of IMP-1 metallo-β-lactamase
    • 68Zn isotope exchange experiments reveal an unusual kinetic lability of the metal ions in the di-zinc form of IMP-1 metallo-β-lactamase. Chem. Commun. 5 (2006) 532-534
    • (2006) Chem. Commun. , vol.5 , pp. 532-534
    • Siemann, S.1    Badiei, H.R.2    Karanassios, V.3    Viswanatha, T.4    Dimitrienko, G.I.5
  • 81
    • 0001415364 scopus 로고
    • Metal detoxification in aquatic organisms
    • Tessier A., and Turner D.R. (Eds), John Wiley, New York
    • Mason A.Z., and Jenkins K. Metal detoxification in aquatic organisms. In: Tessier A., and Turner D.R. (Eds). Metal Speciation and Bioavailability in Aquatic Systems (1995), John Wiley, New York 479-608
    • (1995) Metal Speciation and Bioavailability in Aquatic Systems , pp. 479-608
    • Mason, A.Z.1    Jenkins, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.