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Volumn 25, Issue 14, 2011, Pages 1981-1992

Dissociation of deprotonated microcystin variants by collision-induced dissociation following electrospray ionization

Author keywords

[No Author keywords available]

Indexed keywords

DISSOCIATION; MASS SPECTROMETERS; MASS SPECTROMETRY; NEGATIVE IONS; POSITIVE IONS; TOXIC MATERIALS;

EID: 79959659387     PISSN: 09514198     EISSN: 10970231     Source Type: Journal    
DOI: 10.1002/rcm.5083     Document Type: Article
Times cited : (15)

References (36)
  • 1
    • 0025333146 scopus 로고
    • Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatase-1 and phosphatase-2A from both mammals and higher-plants
    • C. Mackintosh, K. A. Beattie, S. Klumpp, P. Cohen, G. A. Codd,. Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatase-1 and phosphatase-2A from both mammals and higher-plants. FEBS Lett. 1990, 264, 187.
    • (1990) FEBS Lett. , vol.264 , pp. 187
    • MacKintosh, C.1    Beattie, K.A.2    Klumpp, S.3    Cohen, P.4    Codd, G.A.5
  • 4
    • 67649401697 scopus 로고    scopus 로고
    • Development of an analytical method for the unambiguous structure elucidation of cyclic peptides with special appliance for hepatotoxic desmethylated microcystins
    • T. Krüger, B. Christian, B. Luckas,. Development of an analytical method for the unambiguous structure elucidation of cyclic peptides with special appliance for hepatotoxic desmethylated microcystins. Toxicon 2009, 54, 302.
    • (2009) Toxicon , vol.54 , pp. 302
    • Krüger, T.1    Christian, B.2    Luckas, B.3
  • 8
    • 0000483177 scopus 로고
    • Structure and biosynthesis of toxins from blue-green-algae (Cyanobacteria)
    • K. L. Rinehart, M. Namikoshi, B. W. Choi,. Structure and biosynthesis of toxins from blue-green-algae (Cyanobacteria). J. Appl. Phycol. 1994, 6, 159.
    • (1994) J. Appl. Phycol. , vol.6 , pp. 159
    • Rinehart, K.L.1    Namikoshi, M.2    Choi, B.W.3
  • 9
    • 0028117307 scopus 로고
    • Isolation and identification of 12 microcystins from 4 strains and 2 bloom samples of Microcystis spp. - Structure of a new hepatotoxin
    • R. Luukkainen, M. Namikoshi, K. Sivonen, K. L. Rinehart, S. I. Niemela,. Isolation and identification of 12 microcystins from 4 strains and 2 bloom samples of Microcystis spp.-structure of a new hepatotoxin. Toxicon 1994, 32, 133.
    • (1994) Toxicon , vol.32 , pp. 133
    • Luukkainen, R.1    Namikoshi, M.2    Sivonen, K.3    Rinehart, K.L.4    Niemela, S.I.5
  • 10
    • 0027454770 scopus 로고
    • Liquid-chromatography electrospray ionization mass-spectrometry of cyanobacterial toxins
    • G. K. Poon, L. J. Griggs, C. Edwards, K. A. Beattie, G. A. Codd,. Liquid-chromatography electrospray ionization mass-spectrometry of cyanobacterial toxins. J. Chromatogr. 1993, 628, 215.
    • (1993) J. Chromatogr. , vol.628 , pp. 215
    • Poon, G.K.1    Griggs, L.J.2    Edwards, C.3    Beattie, K.A.4    Codd, G.A.5
  • 11
    • 0028787872 scopus 로고
    • Mass-spectral analyses of microcystins from toxic cyanobacteria using online chromatographic and electrophoretic separations
    • K. P. Bateman, P. Thibault, D. J. Douglas, R. L. White,. Mass-spectral analyses of microcystins from toxic cyanobacteria using online chromatographic and electrophoretic separations. J. Chromatogr. A 1995, 712, 253.
    • (1995) J. Chromatogr. A , vol.712 , pp. 253
    • Bateman, K.P.1    Thibault, P.2    Douglas, D.J.3    White, R.L.4
  • 13
    • 0033013004 scopus 로고    scopus 로고
    • Low-energy collisionally activated decomposition and structural characterization of cyclic heptapeptide microcystins by electrospray ionization mass spectrometry
    • M. Yuan, M. Namikoshi, A. Otsuki, K. L. Rinehart, K. Sivonen, M. F. Watanabe,. Low-energy collisionally activated decomposition and structural characterization of cyclic heptapeptide microcystins by electrospray ionization mass spectrometry. J. Mass Spectrom. 1999, 34, 33.
    • (1999) J. Mass Spectrom. , vol.34 , pp. 33
    • Yuan, M.1    Namikoshi, M.2    Otsuki, A.3    Rinehart, K.L.4    Sivonen, K.5    Watanabe, M.F.6
  • 14
    • 0034284175 scopus 로고    scopus 로고
    • Direct analysis of microcystins by microbore liquid chromatography electrospray ionization ion-trap tandem mass spectrometry
    • J. A. Zweigenbaum, J. D. Henion, K. A. Beattie, G. A. Codd, G. K. Poon,. Direct analysis of microcystins by microbore liquid chromatography electrospray ionization ion-trap tandem mass spectrometry. J. Pharm. Biomed. Anal. 2000, 23, 723.
    • (2000) J. Pharm. Biomed. Anal. , vol.23 , pp. 723
    • Zweigenbaum, J.A.1    Henion, J.D.2    Beattie, K.A.3    Codd, G.A.4    Poon, G.K.5
  • 15
    • 14744284334 scopus 로고    scopus 로고
    • Characterization of microcystins using in-source collision-induced dissociation
    • C. Kubwabo, N. Vais, F. M. Benoit,. Characterization of microcystins using in-source collision-induced dissociation. Rapid Commun. Mass Spectrom. 2005, 19, 597.
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 597
    • Kubwabo, C.1    Vais, N.2    Benoit, F.M.3
  • 17
    • 22544456537 scopus 로고    scopus 로고
    • Liquid chromatography-tandem mass spectrometry and accurate m/z measurements of cyclic peptide cyanobacteria toxins
    • C. W. Diehnelt, S. M. Peterman, W. L. Budde,. Liquid chromatography- tandem mass spectrometry and accurate m/z measurements of cyclic peptide cyanobacteria toxins. TrAC Trends Anal. Chem. 2005, 24, 622.
    • (2005) TrAC Trends Anal. Chem. , vol.24 , pp. 622
    • Diehnelt, C.W.1    Peterman, S.M.2    Budde, W.L.3
  • 18
    • 30744459372 scopus 로고    scopus 로고
    • Identification of microcystin toxins from a strain of Microcystis aeruginosa by liquid chromatography introduction into a hybrid linear ion trap-fourier transform ion cyclotron resonance mass spectrometer
    • C. W. Diehnelt, N. R. Dugan, S. M. Peterman, W. L. Budde,. Identification of microcystin toxins from a strain of Microcystis aeruginosa by liquid chromatography introduction into a hybrid linear ion trap-fourier transform ion cyclotron resonance mass spectrometer. Anal. Chem. 2006, 78, 501.
    • (2006) Anal. Chem. , vol.78 , pp. 501
    • Diehnelt, C.W.1    Dugan, N.R.2    Peterman, S.M.3    Budde, W.L.4
  • 19
    • 33846123000 scopus 로고    scopus 로고
    • Structural characterization of microcystins by LC/MS/MS under ion trap conditions
    • T. Mayumi, H. Kato, S. Imanishi, Y. Kawasaki, M. Hasegawa, K. Harada,. Structural characterization of microcystins by LC/MS/MS under ion trap conditions. J. Antibiot. 2006, 59, 710.
    • (2006) J. Antibiot. , vol.59 , pp. 710
    • Mayumi, T.1    Kato, H.2    Imanishi, S.3    Kawasaki, Y.4    Hasegawa, M.5    Harada, K.6
  • 20
    • 0033472947 scopus 로고    scopus 로고
    • Multistep tandem mass spectrometry for sequencing cyclic peptides in an ion-trap mass spectrometer
    • L. C. M. Ngoka, M. L. Gross,. Multistep tandem mass spectrometry for sequencing cyclic peptides in an ion-trap mass spectrometer. J. Am. Soc. Mass Spectrom. 1999, 10, 732.
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 732
    • Ngoka, L.C.M.1    Gross, M.L.2
  • 21
    • 0034778505 scopus 로고    scopus 로고
    • Negative ion fragmentations of deprotonated peptides: Backbone cleavages directed through both Asp and Glu
    • C. S. Brinkworth, S. Dua, A. M. McAnoy, J. H. Bowie,. Negative ion fragmentations of deprotonated peptides: backbone cleavages directed through both Asp and Glu. Rapid Commun. Mass Spectrom. 2001, 15, 1965.
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 1965
    • Brinkworth, C.S.1    Dua, S.2    McAnoy, A.M.3    Bowie, J.H.4
  • 22
    • 67650354095 scopus 로고    scopus 로고
    • Negative ion fragmentations of deprotonated peptides. The unusual case of isoAsp: A joint experimental and theoretical study. Comparison with positive ion cleavages
    • H. J. Andreazza, T. F. Wang, C. J. Bagley, P. Hoffmann, J. H. Bowie,. Negative ion fragmentations of deprotonated peptides. The unusual case of isoAsp: a joint experimental and theoretical study. Comparison with positive ion cleavages. Rapid Commun. Mass Spectrom. 2009, 23, 1993.
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 1993
    • Andreazza, H.J.1    Wang, T.F.2    Bagley, C.J.3    Hoffmann, P.4    Bowie, J.H.5
  • 23
    • 84994921866 scopus 로고
    • Mass-spectrometric determination of the amino-acid sequence of peptides and proteins
    • K. Biemann, S. A. Martin,. Mass-spectrometric determination of the amino-acid sequence of peptides and proteins. Mass Spectrom. Rev. 1987, 6, 1.
    • (1987) Mass Spectrom. Rev. , vol.6 , pp. 1
    • Biemann, K.1    Martin, S.A.2
  • 24
    • 0036489424 scopus 로고    scopus 로고
    • Collision-induced fragmentations of the (M-H)(-) parent anions of underivatized peptides: An aid to structure determination and some unusual negative ion cleavages
    • J. H. Bowie, C. S. Brinkworth, S. Dua,. Collision-induced fragmentations of the (M-H)(-) parent anions of underivatized peptides: An aid to structure determination and some unusual negative ion cleavages. Mass Spectrom. Rev. 2002, 21, 87.
    • (2002) Mass Spectrom. Rev. , vol.21 , pp. 87
    • Bowie, J.H.1    Brinkworth, C.S.2    Dua, S.3
  • 25
    • 59149095292 scopus 로고    scopus 로고
    • Fragmentations of (M-H)(-) anions of underivatised peptides. Part 2: Characteristic cleavages of ser and Cys and of disulfides and other post-translational modifications, together with some unusual internal processes
    • D. Bilusich, J. H. Bowie,. Fragmentations of (M-H)(-) anions of underivatised peptides. Part 2: characteristic cleavages of Ser and Cys and of disulfides and other post-translational modifications, together with some unusual internal processes. Mass Spectrom. Rev. 2009, 28, 20.
    • (2009) Mass Spectrom. Rev. , vol.28 , pp. 20
    • Bilusich, D.1    Bowie, J.H.2
  • 26
    • 0033473718 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometric analysis of microcystins, cyclic heptapeptide hepatotoxins: Modulation of charge states and M+H (+) to M+Na (+) ratio
    • M. Yuan, M. Namikoshi, A. Otsuki, M. F. Watanabe, K. L. Rinehart,. Electrospray ionization mass spectrometric analysis of microcystins, cyclic heptapeptide hepatotoxins: Modulation of charge states and M+H (+) to M+Na (+) ratio. J. Am. Soc. Mass Spectrom. 1999, 10, 1138.
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 1138
    • Yuan, M.1    Namikoshi, M.2    Otsuki, A.3    Watanabe, M.F.4    Rinehart, K.L.5
  • 27
    • 66449102730 scopus 로고    scopus 로고
    • Liquid chromatography coupled to quadruple time-of-flight tandem mass spectrometry for microcystin analysis in freshwaters: Method performances and characterisation of a novel variant of microcystin-RR
    • P. Ferranti, S. Fabbrocino, A. Nasi, S. Caira, M. Bruno, L. Serpe, P. Gallo,. Liquid chromatography coupled to quadruple time-of-flight tandem mass spectrometry for microcystin analysis in freshwaters: method performances and characterisation of a novel variant of microcystin-RR. Rapid Commun. Mass Spectrom. 2009, 23, 1328.
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 1328
    • Ferranti, P.1    Fabbrocino, S.2    Nasi, A.3    Caira, S.4    Bruno, M.5    Serpe, L.6    Gallo, P.7
  • 28
    • 66149104070 scopus 로고    scopus 로고
    • Electrolyte-induced ionization suppression and microcystin toxins: Ammonium formate suppresses sodium replacement ions and enhances protiated and ammoniated ions for improved specificity in quantitative LC-MS-MS
    • W. M. Draper, D. D. Xu, S. K. Perera,. Electrolyte-induced ionization suppression and microcystin toxins: ammonium formate suppresses sodium replacement ions and enhances protiated and ammoniated ions for improved specificity in quantitative LC-MS-MS. Anal. Chem. 2009, 81, 4153.
    • (2009) Anal. Chem. , vol.81 , pp. 4153
    • Draper, W.M.1    Xu, D.D.2    Perera, S.K.3
  • 29
    • 37049080007 scopus 로고
    • Extraction and high-performance liquid-chromatographic method for the determination of microcystins in raw and treated waters
    • L. A. Lawton, C. Edwards, G. A. Codd,. Extraction and high-performance liquid-chromatographic method for the determination of microcystins in raw and treated waters. Analyst 1994, 119, 1525.
    • (1994) Analyst , vol.119 , pp. 1525
    • Lawton, L.A.1    Edwards, C.2    Codd, G.A.3
  • 30
    • 77749285769 scopus 로고    scopus 로고
    • A comparison of positive and negative ion collision-induced dissociation for model heptapeptides with one basic residue
    • D. Pu, N. L. Clipston, C. J. Cassady,. A comparison of positive and negative ion collision-induced dissociation for model heptapeptides with one basic residue. J. Mass Spectrom. 2010, 45, 297.
    • (2010) J. Mass Spectrom. , vol.45 , pp. 297
    • Pu, D.1    Clipston, N.L.2    Cassady, C.J.3
  • 31
    • 0035564364 scopus 로고    scopus 로고
    • Sequence-specific fragmentation of deprotonated peptides containing H or alkyl side chains
    • A. G. Harrison,. Sequence-specific fragmentation of deprotonated peptides containing H or alkyl side chains. J. Am. Soc. Mass Spectrom. 2001, 12, 1.
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 1
    • Harrison, A.G.1
  • 32
    • 0037260331 scopus 로고    scopus 로고
    • Amide bond cleavage in deprotonated tripeptides: A newly discovered pathway to ''b(2) ions
    • A. G. Harrison, K. W. M. Siu, H. El Aribi,. Amide bond cleavage in deprotonated tripeptides: a newly discovered pathway to ''b(2) ions. Rapid Commun. Mass Spectrom. 2003, 17, 869.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 869
    • Harrison, A.G.1    Siu, K.W.M.2    El Aribi, H.3
  • 33
    • 2342505844 scopus 로고    scopus 로고
    • A Hartree-Fock, MP2 and DFT computational study of the structures and energies of ''b(2) ions derived from deprotonated peptides. A comparison of method and basis set used on relative product stabilities
    • G. A. Chass, C. N. J. Marai, D. H. Setiadi, I. G. Csizmadia, A. G. Harrison,. A Hartree-Fock, MP2 and DFT computational study of the structures and energies of ''b(2) ions derived from deprotonated peptides. A comparison of method and basis set used on relative product stabilities. J. Mol. Struct. Theochem 2004, 675, 149.
    • (2004) J. Mol. Struct. Theochem , vol.675 , pp. 149
    • Chass, G.A.1    Marai, C.N.J.2    Setiadi, D.H.3    Csizmadia, I.G.4    Harrison, A.G.5
  • 34
    • 67651027832 scopus 로고    scopus 로고
    • Optimized Orbitrap HCD for Quantitative Analysis of Phosphopeptides
    • Y. Zhang, S. B. Ficarro, S. Li, J. A. Marto,. Optimized Orbitrap HCD for Quantitative Analysis of Phosphopeptides. J. Am. Soc. Mass Spectrom. 2009, 20, 1425.
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 1425
    • Zhang, Y.1    Ficarro, S.B.2    Li, S.3    Marto, J.A.4
  • 35
    • 84989078346 scopus 로고
    • Collision-induced dissociations of deprotonated peptides, dipeptides and tripeptides with hydrogen and alkyl alpha-groups - An aid to structure determination
    • M. Eckersley, J. H. Bowie, R. N. Hayes,. Collision-induced dissociations of deprotonated peptides, dipeptides and tripeptides with hydrogen and alkyl alpha-groups-an aid to structure determination. Org. Mass Spectrom. 1989, 24, 597.
    • (1989) Org. Mass Spectrom. , vol.24 , pp. 597
    • Eckersley, M.1    Bowie, J.H.2    Hayes, R.N.3
  • 36
    • 0034727534 scopus 로고    scopus 로고
    • D-Leu(1) microcystin-LR, from the cyanobacterium Microcystis RST 9501 and from a Microcystis bloom in the Patos Lagoon estuary, Brazil
    • A. Matthiensen, K. A. Beattie, J. S. Yunes, K. Kaya, G. A. Codd,. D-Leu(1) microcystin-LR, from the cyanobacterium Microcystis RST 9501 and from a Microcystis bloom in the Patos Lagoon estuary, Brazil. Phytochemistry 2000, 55, 383.
    • (2000) Phytochemistry , vol.55 , pp. 383
    • Matthiensen, A.1    Beattie, K.A.2    Yunes, J.S.3    Kaya, K.4    Codd, G.A.5


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