메뉴 건너뛰기




Volumn 391, Issue 1, 2009, Pages 74-76

A direct spectrophotometric method for the simultaneous determination of zinc and cobalt in metalloproteins using 4-(2-pyridylazo)resorcinol

Author keywords

[No Author keywords available]

Indexed keywords

COBALT; METAL IONS; PHENOLS; SPECTROPHOTOMETRY; ZINC;

EID: 67349273694     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.05.007     Document Type: Article
Times cited : (39)

References (15)
  • 1
    • 0034633293 scopus 로고    scopus 로고
    • Colorimetric and fluorimetric assays to quantitate micromolar concentrations of transition metals
    • McCall K.A., and Fierke C.A. Colorimetric and fluorimetric assays to quantitate micromolar concentrations of transition metals. Anal. Biochem. 284 (2000) 307-315
    • (2000) Anal. Biochem. , vol.284 , pp. 307-315
    • McCall, K.A.1    Fierke, C.A.2
  • 2
    • 0022051541 scopus 로고
    • The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase
    • Hunt J.B., Neece S.H., and Ginsburg A. The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase. Anal. Biochem. 146 (1985) 150-157
    • (1985) Anal. Biochem. , vol.146 , pp. 150-157
    • Hunt, J.B.1    Neece, S.H.2    Ginsburg, A.3
  • 3
    • 0037014621 scopus 로고    scopus 로고
    • IMP-1 metallo-β-lactamase: Effect of chelators and assessment of metal requirement by electrospray mass spectrometry
    • Siemann S., Brewer D., Clarke A.J., Dmitrienko G.I., Lajoie G., and Viswanatha T. IMP-1 metallo-β-lactamase: Effect of chelators and assessment of metal requirement by electrospray mass spectrometry. Biochim. Biophys. Acta 1571 (2002) 190-200
    • (2002) Biochim. Biophys. Acta , vol.1571 , pp. 190-200
    • Siemann, S.1    Brewer, D.2    Clarke, A.J.3    Dmitrienko, G.I.4    Lajoie, G.5    Viswanatha, T.6
  • 4
    • 53149103974 scopus 로고    scopus 로고
    • Denaturational stress induces formation of zinc-deficient monomers of Cu, Zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis
    • Mulligan V.K., Kerman A., Ho S., and Chakrabartty A. Denaturational stress induces formation of zinc-deficient monomers of Cu, Zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis. J. Mol. Biol. 383 (2008) 424-436
    • (2008) J. Mol. Biol. , vol.383 , pp. 424-436
    • Mulligan, V.K.1    Kerman, A.2    Ho, S.3    Chakrabartty, A.4
  • 6
    • 0032547109 scopus 로고    scopus 로고
    • Simultaneous determination of cobalt(II) and Ni(II) in water and soil samples with sequential injection analysis
    • Taljaard R.E., and van Staden J.F. Simultaneous determination of cobalt(II) and Ni(II) in water and soil samples with sequential injection analysis. Anal. Chim. Acta 366 (1998) 177-186
    • (1998) Anal. Chim. Acta , vol.366 , pp. 177-186
    • Taljaard, R.E.1    van Staden, J.F.2
  • 7
    • 0035690880 scopus 로고    scopus 로고
    • Zinc coordination sphere in biochemical zinc sites
    • Auld D.S. Zinc coordination sphere in biochemical zinc sites. Biometals 14 (2001) 271-313
    • (2001) Biometals , vol.14 , pp. 271-313
    • Auld, D.S.1
  • 8
    • 7744244599 scopus 로고    scopus 로고
    • Recent advances in zinc enzymology
    • Lipscomb W.N., and Sträter N. Recent advances in zinc enzymology. Chem. Rev. 96 (1996) 2375-2434
    • (1996) Chem. Rev. , vol.96 , pp. 2375-2434
    • Lipscomb, W.N.1    Sträter, N.2
  • 9
    • 0021667647 scopus 로고
    • High spin cobalt(II) as a probe for the investigation of metalloproteins
    • Bertini I., and Luchinat C. High spin cobalt(II) as a probe for the investigation of metalloproteins. Adv. Inorg. Biochem. 6 (1984) 71-111
    • (1984) Adv. Inorg. Biochem. , vol.6 , pp. 71-111
    • Bertini, I.1    Luchinat, C.2
  • 10
    • 0029062905 scopus 로고
    • Removal and replacement of metal ions in metallopeptidases
    • Auld D.S. Removal and replacement of metal ions in metallopeptidases. Methods Enzymol. 248 (1995) 228-242
    • (1995) Methods Enzymol. , vol.248 , pp. 228-242
    • Auld, D.S.1
  • 11
    • 0015147652 scopus 로고
    • Spectral properties of cobalt carboxypeptidase: the effects of substrates and inhibitors
    • Latt S.A., and Vallee B.L. Spectral properties of cobalt carboxypeptidase: the effects of substrates and inhibitors. Biochemistry 10 (1971) 4263-4270
    • (1971) Biochemistry , vol.10 , pp. 4263-4270
    • Latt, S.A.1    Vallee, B.L.2
  • 12
    • 0016170446 scopus 로고
    • Metal substitutions and inhibition of thermolysin: spectra of the cobalt enzyme
    • Holmquist B., and Vallee B.L. Metal substitutions and inhibition of thermolysin: spectra of the cobalt enzyme. J. Biol. Chem. 249 (1974) 4601-4607
    • (1974) J. Biol. Chem. , vol.249 , pp. 4601-4607
    • Holmquist, B.1    Vallee, B.L.2
  • 13
    • 0023658624 scopus 로고
    • Electronic spectroscopy of cobalt angiotensin converting enzyme and its inhibitor complexes
    • Bicknell R., Holmquist B., Lee F.S., Martin M.T., and Riordan J.F. Electronic spectroscopy of cobalt angiotensin converting enzyme and its inhibitor complexes. Biochemistry 26 (1987) 7291-7297
    • (1987) Biochemistry , vol.26 , pp. 7291-7297
    • Bicknell, R.1    Holmquist, B.2    Lee, F.S.3    Martin, M.T.4    Riordan, J.F.5
  • 14
    • 0030878054 scopus 로고    scopus 로고
    • Spectroscopically distinct cobalt(II) sites in heterodimetallic forms of the aminopeptidase from Aeromonas proteolytica: characterization of substrate binding
    • Bennett B., and Holz R.C. Spectroscopically distinct cobalt(II) sites in heterodimetallic forms of the aminopeptidase from Aeromonas proteolytica: characterization of substrate binding. Biochemistry 36 (1997) 9837-9846
    • (1997) Biochemistry , vol.36 , pp. 9837-9846
    • Bennett, B.1    Holz, R.C.2
  • 15
    • 54849420301 scopus 로고    scopus 로고
    • Role of the Zn1 and Zn2 sites in metallo-β-lactamase L1
    • Hu Z., Periyannan G., Bennett B., and Crowder M.W. Role of the Zn1 and Zn2 sites in metallo-β-lactamase L1. J. Am. Chem. Soc. 130 (2008) 14207-14216
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14207-14216
    • Hu, Z.1    Periyannan, G.2    Bennett, B.3    Crowder, M.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.