메뉴 건너뛰기




Volumn 47, Issue 8, 2012, Pages 949-961

Qualitative and quantitative characterization of the arsenic-binding behaviour of sulfur-containing peptides and proteins by the coupling of reversed phase liquid chromatography to electrospray ionization mass spectrometry

Author keywords

arsenic binding peptides and proteins; binding constants; folding state; rate constants; reversed phase liquid chromatography coupled to electrospray ionization mass spectrometry

Indexed keywords

APROTININ; BINDING AFFINITIES; BINDING CONSTANT; BINDING STUDIES; CHARGE STATE; CHARGE STATE DISTRIBUTION; CONFORMATIONAL CHANGE; CYSTEINE RESIDUES; CYSTEINE-CONTAINING PEPTIDES; DENATURING CONDITIONS; DIFFERENT SOLVENTS; DISULFIDE BRIDGE; ELECTROSPRAY IONIZATION MASS SPECTROMETRY; FOLDING STATE; HALF LIVES; KINETIC INVESTIGATIONS; LACTOGLOBULIN; LC-ESI-MS; MASS SPECTRA; MILK PROTEIN; MOLTEN GLOBULE; NON-COVALENT INTERACTION; PARTIAL REACTION ORDERS; PROTEIN SPECIES; PROTEIN STRUCTURES; QUANTITATIVE CHARACTERIZATION; REVERSED PHASE LIQUID-CHROMATOGRAPHY; THIOREDOXINS;

EID: 84865213262     PISSN: 10765174     EISSN: 10969888     Source Type: Journal    
DOI: 10.1002/jms.3025     Document Type: Article
Times cited : (6)

References (30)
  • 1
    • 40849147265 scopus 로고    scopus 로고
    • Analytical investigations of phenyl arsenicals in groundwater
    • B. Daus, J. Mattusch, R. Wennrich, H. Weiss,. Analytical investigations of phenyl arsenicals in groundwater. Talanta 2008, 75, 376.
    • (2008) Talanta , vol.75 , pp. 376
    • Daus, B.1    Mattusch, J.2    Wennrich, R.3    Weiss, H.4
  • 2
    • 77956619773 scopus 로고    scopus 로고
    • Concentrations and speciation of arsenic in groundwater polluted by warfare agents
    • B. Daus, M. Hempel, R. Wennrich, H. Weiss,. Concentrations and speciation of arsenic in groundwater polluted by warfare agents. Environ. Pollut. 2010, 158, 3439.
    • (2010) Environ. Pollut. , vol.158 , pp. 3439
    • Daus, B.1    Hempel, M.2    Wennrich, R.3    Weiss, H.4
  • 3
    • 52449145322 scopus 로고    scopus 로고
    • Aquatische Ökotoxizität von Phenylarsinverbindungen-1. Neben- und Umwandlungsprodukte von Blaukreuzkampfstoffen
    • R. Haas, M. Müller, L. Kaminski,. Aquatische Ökotoxizität von Phenylarsinverbindungen-1. Neben- und Umwandlungsprodukte von Blaukreuzkampfstoffen. UWSF-Z. Umweltchem. Ökotox. 1996, 8, 62.
    • (1996) UWSF-Z. Umweltchem. Ökotox , vol.8 , pp. 62
    • Haas, R.1    Müller, M.2    Kaminski, L.3
  • 4
    • 33645856407 scopus 로고    scopus 로고
    • Dithiolproteine als Hüter des intrazellulären Redoxmilieus bei Parasiten: Alte und neue Wirkstoff-Targets bei Trypanosomiasis und Malaria
    • R. L. Krauth-Siegel, H. Bauer, R. H. Schirmer,. Dithiolproteine als Hüter des intrazellulären Redoxmilieus bei Parasiten: alte und neue Wirkstoff-Targets bei Trypanosomiasis und Malaria. Angew. Chem. 2005, 117, 698.
    • (2005) Angew. Chem. , vol.117 , pp. 698
    • Krauth-Siegel, R.L.1    Bauer, H.2    Schirmer, R.H.3
  • 5
    • 4644269993 scopus 로고    scopus 로고
    • Stoffmonographie Arsen-Referenzwert für Urin. Stellungnahme der Kommission "human-Biomonitoring" des Umweltbundesamtes
    • HBM-Kommission
    • HBM-Kommission. Stoffmonographie Arsen-Referenzwert für Urin. Stellungnahme der Kommission "Human-Biomonitoring" des Umweltbundesamtes. Bundesgesundheitsbl. Gesundheitsforsch. Gesundheitsschutz 2003, 46, 1098.
    • (2003) Bundesgesundheitsbl. Gesundheitsforsch. Gesundheitsschutz , vol.46 , pp. 1098
  • 6
    • 0037036578 scopus 로고    scopus 로고
    • Arsenic toxicity and potential mechanisms of action
    • M. F. Hughes,. Arsenic toxicity and potential mechanisms of action. Toxicol. Lett. 2002, 133, 1.
    • (2002) Toxicol. Lett. , vol.133 , pp. 1
    • Hughes, M.F.1
  • 7
    • 33846247876 scopus 로고    scopus 로고
    • Mass spectrometric evidence for different complexes of peptides and proteins with arsenic(III), arsenic(V), copper(II) and zinc(II) species
    • A. C. Schmidt, J. Koppelt, M. Neustadt, M. Otto,. Mass spectrometric evidence for different complexes of peptides and proteins with arsenic(III), arsenic(V), copper(II) and zinc(II) species. Rapid Commun. Mass Spectrom. 2007, 21, 153.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 153
    • Schmidt, A.C.1    Koppelt, J.2    Neustadt, M.3    Otto, M.4
  • 8
    • 34250849710 scopus 로고    scopus 로고
    • Quantitative evaluation of the binding of phenylarsenic species to glutathione, isotocin, and thioredoxin by means of electrospray ionization time-of-flight mass spectrometry
    • A. C. Schmidt, M. Neustadt, M. Otto,. Quantitative evaluation of the binding of phenylarsenic species to glutathione, isotocin, and thioredoxin by means of electrospray ionization time-of-flight mass spectrometry. J. Mass Spectrom. 2007, 42, 771.
    • (2007) J. Mass Spectrom. , vol.42 , pp. 771
    • Schmidt, A.C.1    Neustadt, M.2    Otto, M.3
  • 9
    • 76849095841 scopus 로고    scopus 로고
    • Investigation of the interaction between arsenic species and thiols via electrospray ionization tandem mass spectrometry
    • S. G. Park, D. J. Butcher,. Investigation of the interaction between arsenic species and thiols via electrospray ionization tandem mass spectrometry. Microchem. J. 2010, 95, 57.
    • (2010) Microchem. J. , vol.95 , pp. 57
    • Park, S.G.1    Butcher, D.J.2
  • 10
    • 36248930336 scopus 로고    scopus 로고
    • Study of interactions between arsenicals and thioredoxins (human and E. coli) using mass spectrometry
    • Z. Wang, H. Zhang, X. F. Li, X. C. Le,. Study of interactions between arsenicals and thioredoxins (human and E. coli) using mass spectrometry. Rapid Commun. Mass Spectrom. 2007, 21, 3658.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 3658
    • Wang, Z.1    Zhang, H.2    Li, X.F.3    Le, X.C.4
  • 11
    • 66149131862 scopus 로고    scopus 로고
    • Identification of arsenic-binding proteins in human cells by affinity chromatography and mass spectrometry
    • H. Yan, N. Wang, M. Weinfeld, W. R. Cullen, X. C. Le,. Identification of arsenic-binding proteins in human cells by affinity chromatography and mass spectrometry. Anal. Chem. 2009, 81, 4144.
    • (2009) Anal. Chem. , vol.81 , pp. 4144
    • Yan, H.1    Wang, N.2    Weinfeld, M.3    Cullen, W.R.4    Le, X.C.5
  • 12
    • 57849134123 scopus 로고    scopus 로고
    • Stability of arsenic peptides in plant extracts: Off-line versus on-line parallel elemental and molecular mass spectrometric detection for liquid chromatographic separation
    • K. Bluemlein, A. Raab, J. Feldmann,. Stability of arsenic peptides in plant extracts: off-line versus on-line parallel elemental and molecular mass spectrometric detection for liquid chromatographic separation. Anal. Bioanal. Chem. 2009, 393, 357.
    • (2009) Anal. Bioanal. Chem. , vol.393 , pp. 357
    • Bluemlein, K.1    Raab, A.2    Feldmann, J.3
  • 13
    • 77955908220 scopus 로고    scopus 로고
    • Some critical aspects in the determination of binding constants by electrospray ionization mass spectrometry at the example of arsenic bindings to sulfur containing biomolecules
    • A. C. Schmidt, S. Steier,. Some critical aspects in the determination of binding constants by electrospray ionization mass spectrometry at the example of arsenic bindings to sulfur containing biomolecules. J. Mass Spectrom. 2010, 45, 870.
    • (2010) J. Mass Spectrom. , vol.45 , pp. 870
    • Schmidt, A.C.1    Steier, S.2
  • 14
    • 67649232637 scopus 로고    scopus 로고
    • Size exclusion chromatography coupled to electrospray ionization mass spectrometry for analysis and quantitative characterization of arsenic interactions with peptides and proteins
    • A. C. Schmidt, B. Fahlbusch, M. Otto,. Size exclusion chromatography coupled to electrospray ionization mass spectrometry for analysis and quantitative characterization of arsenic interactions with peptides and proteins. J. Mass Spectrom. 2009, 44, 898.
    • (2009) J. Mass Spectrom. , vol.44 , pp. 898
    • Schmidt, A.C.1    Fahlbusch, B.2    Otto, M.3
  • 15
    • 78650540981 scopus 로고    scopus 로고
    • Optimization of peptide and protein separation with a monolithic reversed-phase column and application to arsenic-binding studies
    • A. C. Schmidt, K. Mickein,. Optimization of peptide and protein separation with a monolithic reversed-phase column and application to arsenic-binding studies. J. Chromatogr. A 2011, 1218, 280.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 280
    • Schmidt, A.C.1    Mickein, K.2
  • 16
    • 39749091910 scopus 로고    scopus 로고
    • Developments in the use and fabrication of organic monolithic phases for use with high-performance liquid chromatography and capillary electrochromatography
    • N. W. Smith, Z. Jiang,. Developments in the use and fabrication of organic monolithic phases for use with high-performance liquid chromatography and capillary electrochromatography. J. Chromatogr. A 2008, 1184, 416.
    • (2008) J. Chromatogr. A , vol.1184 , pp. 416
    • Smith, N.W.1    Jiang, Z.2
  • 17
    • 0032727878 scopus 로고    scopus 로고
    • Rapid reversed-phase separation of proteins and peptides using optimized 'moulded' monolithic poly(styrene-co-divinylbenzene) columns
    • S. Xie, R. W. Allington, F. Svec, J. M. J. Fréchet,. Rapid reversed-phase separation of proteins and peptides using optimized 'moulded' monolithic poly(styrene-co-divinylbenzene) columns. J. Chromatogr. A 1999, 856, 169.
    • (1999) J. Chromatogr. A , vol.856 , pp. 169
    • Xie, S.1    Allington, R.W.2    Svec, F.3    Fréchet, J.M.J.4
  • 18
    • 20444379238 scopus 로고    scopus 로고
    • Arsenite binding to synthetic peptides based on the Zn finger region of the human estrogen receptor-alpha
    • K. T. Kitchin, K. Wallace,. Arsenite binding to synthetic peptides based on the Zn finger region of the human estrogen receptor-alpha. Toxicol. Appl. Pharmacol. 2005, 206, 66.
    • (2005) Toxicol. Appl. Pharmacol. , vol.206 , pp. 66
    • Kitchin, K.T.1    Wallace, K.2
  • 19
    • 33344473169 scopus 로고    scopus 로고
    • Arsenite binding to synthetic peptides: The effect of increasing length between two cysteines
    • K. T. Kitchin, K. Wallace,. Arsenite binding to synthetic peptides: the effect of increasing length between two cysteines. J. Biochem. Mol. Toxicol. 2006, 20, 35.
    • (2006) J. Biochem. Mol. Toxicol. , vol.20 , pp. 35
    • Kitchin, K.T.1    Wallace, K.2
  • 20
    • 0346848892 scopus 로고    scopus 로고
    • The metabolism of inorganic arsenic oxides, gallium arsenide, and arsine: A toxicochemical review
    • D. E. Carter, H. V. Aposhian, A. J. Gandolfi,. The metabolism of inorganic arsenic oxides, gallium arsenide, and arsine: a toxicochemical review. Toxicol. Appl. Pharmacol. 2003, 193, 309.
    • (2003) Toxicol. Appl. Pharmacol. , vol.193 , pp. 309
    • Carter, D.E.1    Aposhian, H.V.2    Gandolfi, A.J.3
  • 21
    • 0033567060 scopus 로고    scopus 로고
    • A comparison between the sulfhydryl reductants tris(2-carboxyethyl) phosphine and dithiothreitol for use in protein biochemistry
    • E. Burmeister Getz, M. Xiao, T. Chakraborty, R. Cooke, P. R. Selvin,. A comparison between the sulfhydryl reductants tris(2-carboxyethyl)phosphine and dithiothreitol for use in protein biochemistry. Anal. Biochem. 1999, 273, 73.
    • (1999) Anal. Biochem. , vol.273 , pp. 73
    • Burmeister Getz, E.1    Xiao, M.2    Chakraborty, T.3    Cooke, R.4    Selvin, P.R.5
  • 23
    • 0023889472 scopus 로고
    • Separation of proteins by reversed-phase high-performance liquid chromatography-II. Optimizing sample pre-treatment and mobile phase conditions
    • K. D. Nugent, W. G. Burton, T. K. Slattery, B. F. Johnson, L. R. Snyder,. Separation of proteins by reversed-phase high-performance liquid chromatography-II. Optimizing sample pre-treatment and mobile phase conditions. J. Chromatogr. 1988, 443, 381.
    • (1988) J. Chromatogr. , vol.443 , pp. 381
    • Nugent, K.D.1    Burton, W.G.2    Slattery, T.K.3    Johnson, B.F.4    Snyder, L.R.5
  • 24
    • 66649085901 scopus 로고    scopus 로고
    • Protein S-S bridge reduction: A raman and computational study of lysozyme interaction with TCEP
    • C. David, S. Foley, M. Enescu,. Protein S-S bridge reduction: a raman and computational study of lysozyme interaction with TCEP. Phys. Chem. Chem. Phys. 2009, 11, 2532.
    • (2009) Phys. Chem. Chem. Phys. , vol.11 , pp. 2532
    • David, C.1    Foley, S.2    Enescu, M.3
  • 25
    • 84984521995 scopus 로고
    • Nomenklatur und einige Eigenschaften der Molkenproteine. 2. Mitteilung: α-lactalbumin, Immunoglobuline, Protease-Peptone, Minorproteine und Enzyme
    • T. Sienkiewicz,. Nomenklatur und einige Eigenschaften der Molkenproteine. 2. Mitteilung: α-lactalbumin, Immunoglobuline, Protease-Peptone, Minorproteine und Enzyme. Die Nahrung 1981, 25, 335.
    • (1981) Die Nahrung , vol.25 , pp. 335
    • Sienkiewicz, T.1
  • 26
    • 84984477766 scopus 로고
    • Nomenklatur und einige Eigenschaften der Molkenproteine. 1. Mitteilung: ß-Lactoglobulin
    • T. Sienkiewicz,. Nomenklatur und einige Eigenschaften der Molkenproteine. 1. Mitteilung: ß-Lactoglobulin. Die Nahrung 1981, 25, 329.
    • (1981) Die Nahrung , vol.25 , pp. 329
    • Sienkiewicz, T.1
  • 27
    • 0025182227 scopus 로고
    • Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond
    • K. Kuwajima, M. Ikeguchi, T. Sugawara, Y. Hiraoka, S. Sugai,. Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond. Biochemistry 1990, 29, 8240.
    • (1990) Biochemistry , vol.29 , pp. 8240
    • Kuwajima, K.1    Ikeguchi, M.2    Sugawara, T.3    Hiraoka, Y.4    Sugai, S.5
  • 28
    • 50049129932 scopus 로고    scopus 로고
    • Kinetische Modellierung der thermischen Denaturierung von α-Lactalbumin im sauren pH-Bereich und in Anwesenheit eines Calcium-Komplexbildners
    • A. Tolkach, U. Kulozik,. Kinetische Modellierung der thermischen Denaturierung von α-Lactalbumin im sauren pH-Bereich und in Anwesenheit eines Calcium-Komplexbildners. Chem. Ing. Tech. 2008, 80, 1165.
    • (2008) Chem. Ing. Tech. , vol.80 , pp. 1165
    • Tolkach, A.1    Kulozik, U.2
  • 29
    • 0034685838 scopus 로고    scopus 로고
    • α-Lactalbumin: Structure and function
    • E. A. Permyakov, L. J. Berliner,. α-Lactalbumin: structure and function. FEBS Lett. 2000, 473, 269.
    • (2000) FEBS Lett. , vol.473 , pp. 269
    • Permyakov, E.A.1    Berliner, L.J.2
  • 30
    • 36649009934 scopus 로고    scopus 로고
    • Evaluation of the thermal history of bovine milk from the lactosylation of whey proteins: An investigation by liquid chromatography-electrospray ionization mass spectrometry
    • I. Losito, T. Carbonara, L. Manaci, F. Palmisano,. Evaluation of the thermal history of bovine milk from the lactosylation of whey proteins: an investigation by liquid chromatography-electrospray ionization mass spectrometry. Anal. Bioanal. Chem. 2007, 389, 2065.
    • (2007) Anal. Bioanal. Chem. , vol.389 , pp. 2065
    • Losito, I.1    Carbonara, T.2    Manaci, L.3    Palmisano, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.