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Volumn 22, Issue 2, 2011, Pages 290-299

Mass spectra and ion collision cross sections of hemoglobin

Author keywords

Collision cross section; Dimers; Hemoglobin; Mass spectrum; Monomers; Oxidation; Tetramers

Indexed keywords

CHARGE STATE; COLLISION CROSS SECTIONS; CROSS SECTION; ION COLLISIONS; MASS SPECTRA; MONOMER IONS; TETRAMERS;

EID: 79952523916     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-010-0026-3     Document Type: Article
Times cited : (12)

References (47)
  • 2
    • 0017130331 scopus 로고
    • 2, and 2, 3- diphosphoglycerate
    • 2, and 2, 3- diphosphoglycerate. Brit. Med. Bull. 32, 209-222 (1976)
    • (1976) Brit. Med. Bull. , vol.32 , pp. 209-222
    • Kilmartin, J.V.1
  • 3
    • 0017364269 scopus 로고
    • Structure of myoglobin refined at 2.0Å resolution
    • Takano, T.: Structure of myoglobin refined at 2.0Å resolution. J. Mol. Biol. 110, 537-584 (1977)
    • (1977) J. Mol. Biol. , vol.110 , pp. 537-584
    • Takano, T.1
  • 5
    • 70349876855 scopus 로고    scopus 로고
    • Mass spectrometry of large complexes
    • Bich, C., Zenobi, R.: Mass spectrometry of large complexes. Curr. Opin. Struct. Biol. 19, 632-639 (2009)
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 632-639
    • Bich, C.1    Zenobi, R.2
  • 6
    • 33646016631 scopus 로고    scopus 로고
    • Mass spectrometry in the study of hemoglobin: From covalent structure to higher order assembly
    • Griffith, W.P., Kaltashov, I.A.: Mass spectrometry in the study of hemoglobin: from covalent structure to higher order assembly. Curr. Org. Chem. 10, 535-553 (2006)
    • (2006) Curr. Org. Chem. , vol.10 , pp. 535-553
    • Griffith, W.P.1    Kaltashov, I.A.2
  • 7
    • 62149117617 scopus 로고    scopus 로고
    • Probing hemoglobin structure by means of traveling-wave ion mobility mass spectrometry
    • Scarff, C.A., Patel, V.J., Thalassinos, K., Scrivens, J.H.: Probing hemoglobin structure by means of traveling-wave ion mobility mass spectrometry. J. Am. Soc. Mass Spectrom. 20, 625-631 (2009)
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 625-631
    • Scarff, C.A.1    Patel, V.J.2    Thalassinos, K.3    Scrivens, J.H.4
  • 8
    • 60649117125 scopus 로고    scopus 로고
    • Gas-phase H/D exchange and collision cross sections of hemoglobin monomers, dimers and tetramers
    • Wright, P.J., Douglas, D.J.: Gas-phase H/D exchange and collision cross sections of hemoglobin monomers, dimers and tetramers. J. Am. Soc. Mass Spectrom. 20, 484-495 (2009)
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 484-495
    • Wright, P.J.1    Douglas, D.J.2
  • 9
    • 34548768193 scopus 로고    scopus 로고
    • Symmetric behavior of hemoglobin α- and β- subunits during acid-induced denaturation observed by electrospray mass spectrometry
    • Boys, B.L., Kuprowski, M.C., Konermann, L.: Symmetric behavior of hemoglobin α- and β- subunits during acid-induced denaturation observed by electrospray mass spectrometry. Biochemistry 46, 10675-10684 (2007)
    • (2007) Biochemistry , vol.46 , pp. 10675-10684
    • Boys, B.L.1    Kuprowski, M.C.2    Konermann, L.3
  • 10
    • 0041471397 scopus 로고    scopus 로고
    • Highly asymmetric interactions between globin chains during hemoglobin assembly revealed by electrospray ionization mass spectrometry
    • Griffith, W.P., Kaltashov, I.A.: Highly asymmetric interactions between globin chains during hemoglobin assembly revealed by electrospray ionization mass spectrometry. Biochemistry 42, 10024-10033 (2003)
    • (2003) Biochemistry , vol.42 , pp. 10024-10033
    • Griffith, W.P.1    Kaltashov, I.A.2
  • 14
    • 58149182318 scopus 로고    scopus 로고
    • Traveling wave ion mobility mass spectrometry studies of protein structure: Biological significance and comparison with x-ray crystallography and nuclear magnetic resonance spectroscopy measurements
    • Scarff, C.A., Thalassinos, K., Hilton, G.R., Scrivens, J.H.: Traveling wave ion mobility mass spectrometry studies of protein structure: biological significance and comparison with x-ray crystallography and nuclear magnetic resonance spectroscopy measurements. Rapid Commun. Mass Spectrom. 22, 3297-3304 (2008)
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 3297-3304
    • Scarff, C.A.1    Thalassinos, K.2    Hilton, G.R.3    Scrivens, J.H.4
  • 15
    • 0001686153 scopus 로고
    • Collision cross sections for protein ions
    • Covey, T., Douglas, D.J.: Collision cross sections for protein ions. J. Am. Soc. Mass Spectrom. 4, 616-623 (1993)
    • (1993) J. Am. Soc. Mass Spectrom. , vol.4 , pp. 616-623
    • Covey, T.1    Douglas, D.J.2
  • 16
    • 0031195030 scopus 로고    scopus 로고
    • Collision cross sections of myoglobin and cytochrome c Ions with Ne, Ar, and Kr
    • Chen, Y., Collings, B.A., Douglas, D.J.: Collision cross sections of myoglobin and cytochrome c Ions with Ne, Ar, and Kr. J. Am. Soc. Mass Spectrom. 8, 681-687 (1997)
    • (1997) J. Am. Soc. Mass Spectrom. , vol.8 , pp. 681-687
    • Chen, Y.1    Collings, B.A.2    Douglas, D.J.3
  • 17
    • 33644748260 scopus 로고    scopus 로고
    • Pulsed hydrogen/deuterium exchange MS/MS for studying the relationship between noncovalent protein complexes in solution and in the gas phase after electrospray ionization
    • Hossain, B.M., Konermann, L.: Pulsed hydrogen/deuterium exchange MS/MS for studying the relationship between noncovalent protein complexes in solution and in the gas phase after electrospray ionization. Anal. Chem. 78, 1613-1619 (2006)
    • (2006) Anal. Chem. , vol.78 , pp. 1613-1619
    • Hossain, B.M.1    Konermann, L.2
  • 18
    • 8744221645 scopus 로고    scopus 로고
    • Subunit disassembly and unfolding kinetics of hemoglobin studied by time-resolved electrospray mass spectrometry
    • Simmons, D.A., Wilson, D.J., Lajoie, G.A., Doherty-Kirby, A., Konermann, L.: Subunit disassembly and unfolding kinetics of hemoglobin studied by time-resolved electrospray mass spectrometry. Biochemistry 43, 14792-14801 (2004)
    • (2004) Biochemistry , vol.43 , pp. 14792-14801
    • Simmons, D.A.1    Wilson, D.J.2    Lajoie, G.A.3    Doherty-Kirby, A.4    Konermann, L.5
  • 19
    • 0031050772 scopus 로고    scopus 로고
    • Dissociation of heme from myoglobin and cytochrome b5: Comparison of behavior in solution and in the gas phase
    • Hunter, C.L., Mauk, A.G., Douglas, D.J.: Dissociation of heme from myoglobin and cytochrome b5: comparison of behavior in solution and in the gas phase. Biochemistry 36, 1018-1025 (1997)
    • (1997) Biochemistry , vol.36 , pp. 1018-1025
    • Hunter, C.L.1    Mauk, A.G.2    Douglas, D.J.3
  • 20
    • 0036099232 scopus 로고    scopus 로고
    • Tandem mass spectrometry of protein-protein complexes: Cytochrome c-cytochrome b5
    • Mauk, M.R., Mauk, A.G., Chen, Y.L., Douglas, D.J.: Tandem mass spectrometry of protein-protein complexes: cytochrome c-cytochrome b5. J. Am. Soc. Mass Spectrom. 13, 59-71 (2002)
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13 , pp. 59-71
    • Mauk, M.R.1    Mauk, A.G.2    Chen, Y.L.3    Douglas, D.J.4
  • 21
    • 44049116161 scopus 로고
    • Collisional focusing effects in radiofrequency quadrupoles
    • Douglas, D.J., French, J.B.: Collisional focusing effects in radiofrequency quadrupoles. J. Am. Soc. Mass Spectrom. 3, 398-408 (1992)
    • (1992) J. Am. Soc. Mass Spectrom. , vol.3 , pp. 398-408
    • Douglas, D.J.1    French, J.B.2
  • 22
    • 0001060654 scopus 로고
    • An improved quadrupole mass analyzer
    • Brubaker, W.M.: An improved quadrupole mass analyzer. Adv. Mass Spectrom. 4, 293-299 (1968)
    • (1968) Adv. Mass Spectrom. , vol.4 , pp. 293-299
    • Brubaker, W.M.1
  • 23
    • 0037444531 scopus 로고    scopus 로고
    • Conformations of gas phase lysozyme ions formed from two different solution folding states
    • Mao, D.M., Babu, K.R., Chen, Y.L., Douglas, D.J.: Conformations of gas phase lysozyme ions formed from two different solution folding states. Anal. Chem. 75, 1325-1330 (2003)
    • (2003) Anal. Chem. , vol.75 , pp. 1325-1330
    • Mao, D.M.1    Babu, K.R.2    Chen, Y.L.3    Douglas, D.J.4
  • 24
    • 0002892789 scopus 로고
    • An aerodynamic drag model for protein ions
    • Douglas, D.J.: An aerodynamic drag model for protein ions. J. Am. Soc. Mass Spectrom. 5, 17-18 (1994)
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 17-18
    • Douglas, D.J.1
  • 25
    • 0006739227 scopus 로고
    • Spectrophotometric method for the simultaneous determination of myoglobin and hemoglobin in extracts of human muscle
    • Duve, C.A.: Spectrophotometric method for the simultaneous determination of myoglobin and hemoglobin in extracts of human muscle. Acta Chem. Scand. 2, 264-289 (1948)
    • (1948) Acta Chem. Scand. , vol.2 , pp. 264-289
    • Duve, C.A.1
  • 26
    • 0000756628 scopus 로고
    • The molar light absorption of pyridine ferroprotoporphyrin (pyridine haemochromogen)
    • Paul, K.G., Theorell, H., Akeson, A.: The molar light absorption of pyridine ferroprotoporphyrin (pyridine haemochromogen). Acta Chem. Scand. 7, 1284-1287 (1953)
    • (1953) Acta Chem. Scand. , vol.7 , pp. 1284-1287
    • Paul, K.G.1    Theorell, H.2    Akeson, A.3
  • 27
    • 0007040080 scopus 로고
    • Studies on the oxidation-reduction potentials of heme proteins. IV. The kinetics of oxidation of hemoglobin and myoglobin by ferricyanide
    • Antonini, E., Brunori, M., Wyman, J.: Studies on the oxidation-reduction potentials of heme proteins. IV. The kinetics of oxidation of hemoglobin and myoglobin by ferricyanide. Biochemistry 4, 545-551 (1965)
    • (1965) Biochemistry , vol.4 , pp. 545-551
    • Antonini, E.1    Brunori, M.2    Wyman, J.3
  • 29
    • 0016613465 scopus 로고
    • The molecular dissociation of ferrihemoglobin derivatives
    • White, S.L.: The molecular dissociation of ferrihemoglobin derivatives. J. Biol. Chem 250, 1263-1268 (1975)
    • (1975) J. Biol. Chem , vol.250 , pp. 1263-1268
    • White, S.L.1
  • 31
    • 0022633617 scopus 로고
    • Dissociation of dimers of human hemoglobins A and F into monomers
    • Mrabet, N.T., Shaeffer, J.R., McDonald, M.J., Bunn, H.F.: Dissociation of dimers of human hemoglobins A and F into monomers. J. Biol. Chem. 261, 1111-1115 (1986)
    • (1986) J. Biol. Chem. , vol.261 , pp. 1111-1115
    • Mrabet, N.T.1    Shaeffer, J.R.2    McDonald, M.J.3    Bunn, H.F.4
  • 32
    • 0014940101 scopus 로고
    • Functional aspects of the subunit association-dissociation equilibria of hemoglobin
    • Edelstein, S.J., Rehmar, M.J., Olson, J.S., Gibson, Q.H.: Functional aspects of the subunit association-dissociation equilibria of hemoglobin. J. Biol. Chem. 245, 4372-4381 (1970)
    • (1970) J. Biol. Chem. , vol.245 , pp. 4372-4381
    • Edelstein, S.J.1    Rehmar, M.J.2    Olson, J.S.3    Gibson, Q.H.4
  • 33
    • 0017352615 scopus 로고
    • Thermodynamic studies on subunit assembly in human hemoglobin
    • Ip, S.H.C., Ackers, G.K.: Thermodynamic studies on subunit assembly in human hemoglobin. J. Biol. Chem. 252, 82-87 (1977)
    • (1977) J. Biol. Chem , vol.252 , pp. 82-87
    • Ip, S.H.C.1    Ackers, G.K.2
  • 34
    • 25844522757 scopus 로고    scopus 로고
    • Improved preservation of human red blood cells by lyophilization
    • Han, Y., Quan, G.B., Liu, X.Z., Ma, E.P., Liu, A., Jin, P., Cao, W.: Improved preservation of human red blood cells by lyophilization. Cryobiology 51, 152-164 (2005)
    • (2005) Cryobiology , vol.51 , pp. 152-164
    • Han, Y.1    Quan, G.B.2    Liu, X.Z.3    Ma, E.P.4    Liu, A.5    Jin, P.6    Cao, W.7
  • 35
    • 0025793265 scopus 로고
    • The effects of formulation variables on the stability of freeze-dried human growth hormone
    • Pikal, M.J., Dellerman, K.M., Roy, M.L., Riggin, R.M.: The effects of formulation variables on the stability of freeze-dried human growth hormone. Pharm. Res. 8, 427-436 (1991)
    • (1991) Pharm. Res. , vol.8 , pp. 427-436
    • Pikal, M.J.1    Dellerman, K.M.2    Roy, M.L.3    Riggin, R.M.4
  • 36
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • Vogt, W.: Oxidation of methionyl residues in proteins: tools, targets, and reversal. Free Radic. Biol. Med. 18, 93-105 (1995)
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 93-105
    • Vogt, W.1
  • 37
    • 38849105589 scopus 로고    scopus 로고
    • 2/nitrite-induced post- translational modifications of human hemoglobin determined by mass spectrometry: Redox regulation of tyrosine nitration and 3-nitro tyrosine reduction by antioxidants
    • 2/nitrite-induced post- translational modifications of human hemoglobin determined by mass spectrometry: redox regulation of tyrosine nitration and 3-nitro tyrosine reduction by antioxidants. Chembiochem 9, 312-323 (2008)
    • (2008) Chembiochem , vol.9 , pp. 312-323
    • Chen, H.1    Chang, C.2    Lin, W.3    Cheng, D.4    Leong, M.5
  • 38
    • 70149092747 scopus 로고    scopus 로고
    • Coupling oxidative signals to protein phosphorylation via methionine oxidation in arabidopsis
    • Hardin, S.C., Larue, C.T., Oh, M.H., Jain, V., Huber, S.C.: Coupling oxidative signals to protein phosphorylation via methionine oxidation in arabidopsis. Biochem. J. 422, 305-312 (2009)
    • (2009) Biochem. J. , vol.422 , pp. 305-312
    • Hardin, S.C.1    Larue, C.T.2    Oh, M.H.3    Jain, V.4    Huber, S.C.5
  • 39
    • 0019795646 scopus 로고
    • Hydroxyl radical production in body fluids. Roles of metal ions, ascorbate, and superoxide
    • Winterbourn, C.C.: Hydroxyl radical production in body fluids. Roles of metal ions, ascorbate, and superoxide. Biochem. J. 198, 125-131 (1981)
    • (1981) Biochem. J. , vol.198 , pp. 125-131
    • Winterbourn, C.C.1
  • 40
    • 69749120545 scopus 로고    scopus 로고
    • Cold chemical oxidation of proteins
    • Hambly, D.M., Gross, M.L.: Cold chemical oxidation of proteins. Anal. Chem. 81, 7235-7242 (2009)
    • (2009) Anal. Chem. , vol.81 , pp. 7235-7242
    • Hambly, D.M.1    Gross, M.L.2
  • 41
    • 0030952676 scopus 로고    scopus 로고
    • Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems
    • Chao, C., Ma, Y., Stadtman, E.R.: Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems. Proc. Natl. Acad. Sci. U. S. A. 94, 2969-2974 (1997)
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2969-2974
    • Chao, C.1    Ma, Y.2    Stadtman, E.R.3
  • 42
    • 0141571313 scopus 로고    scopus 로고
    • High-resolution wide-angle x-ray scattering of protein solutions: Effect of beam dose on protein integrity
    • Fischetti, R.F., Rodi, D.J., Mirza, A., Irving, T.C., Kondrashkina, E., Makowski, L.: High-resolution wide-angle x-ray scattering of protein solutions: effect of beam dose on protein integrity. J. Synchrotron. Rad. 10, 398-404 (2003)
    • (2003) J. Synchrotron. Rad. , vol.10 , pp. 398-404
    • Fischetti, R.F.1    Rodi, D.J.2    Mirza, A.3    Irving, T.C.4    Kondrashkina, E.5    Makowski, L.6
  • 44
    • 0014940352 scopus 로고
    • Gel chromatography of proteins in denaturing solvents - Comparison between sodium dodecyl sulfate and guanidine hydrochloride as denaturants
    • Fish, W.W., Reynolds, J.A., Tanford, C.: Gel chromatography of proteins in denaturing solvents - comparison between sodium dodecyl sulfate and guanidine hydrochloride as denaturants. J. Biol. Chem. 245, 5166-5168 (1970)
    • (1970) J. Biol. Chem. , vol.245 , pp. 5166-5168
    • Fish, W.W.1    Reynolds, J.A.2    Tanford, C.3
  • 45
    • 0014851222 scopus 로고
    • Amp Nucleosidase from Azotobacter vinelandii. II. Association and Dissociation
    • Ogasawar, N., Yoshino, M., Asai, J.P.: Amp Nucleosidase from Azotobacter vinelandii. II. Association and Dissociation. J. Biochem. 68, 331-340 (1970)
    • (1970) J. Biochem. , vol.68 , pp. 331-340
    • Ogasawar, N.1    Yoshino, M.2    Asai, J.P.3
  • 46
    • 0021260706 scopus 로고
    • Iodothyronines: Oxidative deiodination by hemoglobin and inhibition of lipid peroxidation
    • Tseng, Y.L., Latham, K.R.: Iodothyronines: oxidative deiodination by hemoglobin and inhibition of lipid peroxidation. Lipids 19, 96-102 (1984)
    • (1984) Lipids , vol.19 , pp. 96-102
    • Tseng, Y.L.1    Latham, K.R.2
  • 47
    • 0032052216 scopus 로고    scopus 로고
    • Hemoglobins from bacteria to man: Evolution of different patterns of gene expression
    • Hardison, R.: Hemoglobins from bacteria to man: evolution of different patterns of gene expression. J. Exp. Biol. 201, 1099-1117 (1998)
    • (1998) J. Exp. Biol. , vol.201 , pp. 1099-1117
    • Hardison, R.1


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