메뉴 건너뛰기




Volumn 22, Issue 7, 2011, Pages 1187-1196

Gas-phase ions of human hemoglobin A, F, and S

Author keywords

Conformation; Cross sections; Hemoglobin; Hydrogen deuterium exchange; MS MS; Protein protein complex

Indexed keywords

COLLISION CROSS SECTIONS; CROSS SECTION; GAS PHASE IONS; GASPHASE; HUMAN HEMOGLOBIN A; HYDROGEN EXCHANGE; HYDROGEN/DEUTERIUM EXCHANGE; INTERNAL ENERGIES; MASS SPECTRA; MS/MS; PROTEIN-PROTEIN COMPLEXES; SINGLE MUTATION; TANDEM MASS SPECTROMETRY; TETRAMERS;

EID: 79959926419     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-011-0138-4     Document Type: Article
Times cited : (11)

References (61)
  • 2
    • 0014803041 scopus 로고
    • Interaction of 2, 3-diphosphoglycerate with various human hemoglobins
    • Bunn, H. F., Briehl, R. W.: Interaction of 2, 3-Diphosphoglycerate with Various Human Hemoglobins. J. Clin. Invest. 49, 1088-1095(1990)
    • (1990) J. Clin. Invest. , vol.49 , pp. 1088-1095
    • Bunn, H.F.1    Briehl, R.W.2
  • 3
    • 0031469017 scopus 로고    scopus 로고
    • Exchange of subunit interfaces between recombinant adult and fetal hemoglobins. Evidence for a functional inter-relationship among regions of the tetramer
    • DOI 10.1074/jbc.272.50.31326
    • Dumoulin, A., Manning, L. R., Jenkins, W. T., Winslow, R. M., Manning, J. M.: Exchange of Subunit Interfaces Between Recombinant Adult and Fetal Hemoglobins-Evidence for a Functional Inter-Relationship Among Regions of the Tetramer. J. Biol. Chem. 272, 31326-31332(1997) (Pubitemid 28013266)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.50 , pp. 31326-31332
    • Dumoulin, A.1    Manning, L.R.2    Jenkins, W.T.3    Winslow, R.M.4    Manning, J.M.5
  • 4
    • 0022633617 scopus 로고    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(1996)
    • (1996) J. Biol. Chem. , vol.261 , pp. 1111-1115
    • Mrabet, N.T.1    Shaeffer, J.R.2    McDonald, M.J.3    Bunn, H.F.4
  • 5
    • 0036295816 scopus 로고    scopus 로고
    • Hemoglobin equilibrium analysis by the multiangle laser light-scattering method
    • DOI 10.1006/bbrc.2002.6362
    • Yamaguchi, T., Adachi, K.: Hemoglobin Equilibrium Analysis by the Multiangle Laser Light-Scattering Method. Biochem. Biophys. Res. Commun. 290, 1382-1387(2002) (Pubitemid 34687410)
    • (2002) Biochemical and Biophysical Research Communications , vol.290 , Issue.5 , pp. 1382-1387
    • Yamaguchi, T.1    Adachi, K.2
  • 6
    • 0014102102 scopus 로고    scopus 로고
    • Structure of sickle cell hemoglobin and molecular mechanism of sickling phenomenon
    • Murayama, M.: Structure of Sickle Cell Hemoglobin and Molecular Mechanism of Sickling Phenomenon. Clin. Chem. 13, 578-588(1997)
    • (1997) Clin. Chem. , vol.13 , pp. 578-588
    • Murayama, M.1
  • 9
    • 41449112582 scopus 로고    scopus 로고
    • Hydroxyurea for the treatment of sickle cell anemia
    • Platt, O. S.: Hydroxyurea for the Treatment of Sickle Cell Anemia. N. Engl. J. Med. 358, 1362-1369(2008)
    • (2008) N. Engl. J. Med. , vol.358 , pp. 1362-1369
    • Platt, O.S.1
  • 10
    • 0032584670 scopus 로고    scopus 로고
    • Normal and abnormal protein subunit interactions in hemoglobins
    • DOI 10.1074/jbc.273.31.19359
    • Manning, J. M., Dumoulin, A., Li, X. F., Manning, L. R.: Normal and Abnormal Protein Subunit Interactions in Hemoglobins. J. Biol. Chem. 273, 19359-19362(1998) (Pubitemid 28366978)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.31 , pp. 19359-19362
    • Manning, J.M.1    Dumoulin, A.2    Li, X.3    Manning, L.R.4
  • 11
    • 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
  • 12
    • 51849166914 scopus 로고    scopus 로고
    • Fetal hemoglobin: Assessment of glycation and acetylation status by electrospray ionization mass spectrometry
    • Davison, A. S., Green, B. N., Roberts, N. B.: Fetal Hemoglobin: Assessment of Glycation and Acetylation Status by Electrospray Ionization Mass Spectrometry. Clin. Chem. Lab. Med. 46, 1230-1238(2008)
    • (2008) Clin. Chem. Lab. Med. , vol.46 , pp. 1230-1238
    • Davison, A.S.1    Green, B.N.2    Roberts, N.B.3
  • 13
    • 36749075723 scopus 로고    scopus 로고
    • Electrospray mass spectrometric characterization of hemoglobin Q (Hb Q-India) and a double mutant hemoglobin S/D in clinical samples
    • DOI 10.1016/j.clinbiochem.2007.09.006, PII S0009912007003621
    • Mandal, A. K., Bisht, S., Bhat, V. S., Krishnaswamy, P. R., Balaram, P.: Electrospray Mass Spectrometric Characterization of Hemoglobin Q (Hb Q-India) and a Double Mutant Hemoglobin S/D in Clinical Samples. Clin. Biochem. 41, 75-81(2008) (Pubitemid 350216826)
    • (2008) Clinical Biochemistry , vol.41 , Issue.1-2 , pp. 75-81
    • Mandal, A.K.1    Bisht, S.2    Bhat, V.S.3    Krishnaswamy, P.R.4    Balaram, P.5
  • 15
    • 58149182319 scopus 로고    scopus 로고
    • Ion mobility augments the utility of mass spectrometry in the identification of human hemoglobin variants
    • Williams, J. P., Giles, K., Green, B. N., Scrivens, J. H., Bateman, R. H.: Ion Mobility Augments the Utility of Mass Spectrometry in the Identification of Human Hemoglobin Variants. Rapid Commun. Mass Spectrom. 22, 3179-3186(2008)
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 3179-3186
    • Williams, J.P.1    Giles, K.2    Green, B.N.3    Scrivens, J.H.4    Bateman, R.H.5
  • 16
    • 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
  • 17
    • 79952523916 scopus 로고    scopus 로고
    • Mass spectra and ion collision cross sections of hemoglobin
    • Kang, Y., Douglas, D. J.: Mass Spectra and Ion Collision Cross Sections of Hemoglobin. J. Am. Soc. Mass Spectrom. 20, 290-299(2001)
    • (2001) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 290-299
    • Kang, Y.1    Douglas, D.J.2
  • 18
    • 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
  • 19
    • 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
    • DOI 10.1021/ac051687e
    • 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) (Pubitemid 43346300)
    • (2006) Analytical Chemistry , vol.78 , Issue.5 , pp. 1613-1619
    • Hossain, B.M.1    Konermann, L.2
  • 20
    • 0035984339 scopus 로고    scopus 로고
    • Studies of biomolecular conformations and conformational dynamics by mass spectrometry
    • DOI 10.1002/mas.10017
    • Kaltashov, I. A., Eyles, S. J.: Studies of Biomolecular Conformations and Conformational Dynamics by Mass Spectrometry. Mass Spectrom. Rev. 21, 37-71(2002) (Pubitemid 34950940)
    • (2002) Mass Spectrometry Reviews , vol.21 , Issue.1 , pp. 37-71
    • Kaltashov, I.A.1    Eyles, S.J.2
  • 21
    • 0033403977 scopus 로고    scopus 로고
    • Gas phase conformations of biological molecules: The hydrogen/deuterium exchange mechanism
    • DOI 10.1016/S1044-0305(98)00121-4, PII S1044030598001214
    • Wyttenbach, T., Bowers, M. T.: Gas Phase Conformations of Biological Molecules: The Hydrogen/Deuterium Exchange Mechanism. J. Am. Soc. Mass Spectrom. 10, 9-14(1999) (Pubitemid 34464082)
    • (1999) Journal of the American Society for Mass Spectrometry , vol.10 , Issue.1 , pp. 9-14
    • Wyttenbach, T.1    Bowers, M.T.2
  • 22
    • 2442637587 scopus 로고    scopus 로고
    • 3: Exchange kinetics do not reflect parent ion structures
    • DOI 10.1021/ja049834y
    • Cox, H. A., Julian, R. R., Lee, S. W., Beauchamp, J. L.: Gas-Phase H/D Exchange of Sodiated Glycine Oligomers with ND3: Exchange Kinetics Do Not Reflect Parent Ion Structures. J. Am. Chem. Soc. 126, 6485-6490(2004) (Pubitemid 38657072)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.20 , pp. 6485-6490
    • Cox, H.A.1    Julian, R.R.2    Lee, S.-W.3    Beauchamp, J.L.4
  • 23
    • 0037213801 scopus 로고    scopus 로고
    • Gas phase hydrogen/deuterium exchange of proteins in an ion trap mass spectrometer
    • Evans, S. E., Lueck, N., Marzluff, E. M.: Gas Phase Hydrogen/Deuterium Exchange of Proteins in an Ion Trap Mass Spectrometer. Int. J. Mass Spectrom. 222, 175-187(2003)
    • (2003) Int. J. Mass Spectrom. , vol.222 , pp. 175-187
    • Evans, S.E.1    Lueck, N.2    Marzluff, E.M.3
  • 24
    • 0030986331 scopus 로고    scopus 로고
    • H/D exchange levels of shape-resolved cytochrome c conformers in the gas phase
    • DOI 10.1021/ja9626751, PII S0002786396026753
    • Valentine, S. J., Clemmer, D. E.: H/D Exchange Levels of Shape-Resolved Cytochrome c Conformers in the Gas Phase. J. Am. Chem. Soc. 119, 3558-3566(1997) (Pubitemid 27226054)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.15 , pp. 3558-3566
    • Valentine, S.J.1    Clemmer, D.E.2
  • 25
    • 0036580728 scopus 로고    scopus 로고
    • Temperature-dependent H/D exchange of compact and elongated cytochrome c ions in the gas phase
    • DOI 10.1016/S1044-0305(02)00372-0, PII S1044030502003720, NoS.
    • Valentine, S. J., Clemmer, D. E.: Temperature-Dependent H/D Exchange of Compact and Elongated Cytochrome c Ions in the Gas Phase. J. Am. Soc. Mass Spectrom. 13, 506-517(2002) (Pubitemid 36870945)
    • (2002) Journal of the American Society for Mass Spectrometry , vol.13 , Issue.5 , pp. 506-517
    • Valentine, S.J.1    Clemmer, D.E.2
  • 26
    • 0033566201 scopus 로고    scopus 로고
    • Assessing the relative stabilities of engineered hemoglobins using electrospray mass spectrometry
    • DOI 10.1006/abio.1999.4140
    • Apostol, I.: Assessing the Relative Stabilities of Engineered Hemoglobins Using Electrospray Mass Spectrometry. Anal. Biochem. 272, 8-18(1999) (Pubitemid 29343376)
    • (1999) Analytical Biochemistry , vol.272 , Issue.1 , pp. 8-18
    • Apostol, I.1
  • 27
    • 0035860204 scopus 로고    scopus 로고
    • Gas-phase dissociation of hemoglobin
    • DOI 10.1016/S1387-3806(01)00428-6, PII S1387380601004286
    • Versluis, C., Heck, A. J. R.: Gas-Phase Dissociation of Hemoglobin. Int. J. Mass Spectrom. 210, 637-649(2001) (Pubitemid 32947131)
    • (2001) International Journal of Mass Spectrometry , vol.210-211 , pp. 637-649
    • Versluis, C.1    Heck, A.J.R.2
  • 28
    • 0019798175 scopus 로고
    • Changes in intermediate hemoglobins during autoxidation of hemoglobin
    • Tomoda, A., Yoneyama, Y., Tsuji, A.: Changes in Intermediate Hemoglobins During Autoxidation of Hemoglobin. Biochem. J. 195, 485-492(1991)
    • (1991) Biochem. J. , vol.195 , pp. 485-492
    • Tomoda, A.1    Yoneyama, Y.2    Tsuji, A.3
  • 29
    • 0031763316 scopus 로고    scopus 로고
    • A new linear ion trap time-of-flight system with tandem mass spectrometry capabilities
    • DOI 10.1002/(SICI)1097-0231(19981030)12:20<1463::AID-RCM357>3.0. CO;2-H
    • Campbell, J. M., Collings, B. A., Douglas, D. J.: A New Linear Ion Trap Time-of-Flight System with Tandem Mass Spectrometry Capabilities. Rapid Commun. Mass Spectrom. 12, 1463-1474(1998) (Pubitemid 28485971)
    • (1998) Rapid Communications in Mass Spectrometry , vol.12 , Issue.20 , pp. 1463-1474
    • Campbell, J.M.1    Collings, B.A.2    Douglas, D.J.3
  • 31
    • 0036390717 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange of myoglobin ions in a linear quadrupole ion trap
    • Mao, D. M., Ding, C. F., Douglas, D. J.: Hydrogen/Deuterium Exchange of Myoglobin Ions in a Linear Quadrupole Ion Trap. Rapid Commun. Mass Spectrom. 16, 1941-1945(2002)
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 1941-1945
    • Mao, D.M.1    Ding, C.F.2    Douglas, D.J.3
  • 32
    • 0037444531 scopus 로고    scopus 로고
    • Conformations of gas-phase lysozyme ions produced from two different solution conformations
    • DOI 10.1021/ac020647x
    • Mao, D. M., Babu, K. R., Chen, Y. L., Douglas, D. J.: Conformations of Gas-Phase Lysozyme Ions Produced from Two Different Solution Conformations. Anal. Chem. 75, 1325-1330(2003) (Pubitemid 36397163)
    • (2003) Analytical Chemistry , vol.75 , Issue.6 , pp. 1325-1330
    • Mao, D.1    Babu, K.R.2    Chen, Y.-L.3    Douglas, D.J.4
  • 33
    • 0031195030 scopus 로고    scopus 로고
    • Collision cross sections of myoglobin and cytochrome c ions with Ne, Ar, and Kr
    • DOI 10.1016/S1044-0305(97)00033-0, PII S1044030597000330
    • Chen, Y. L., 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) (Pubitemid 27263989)
    • (1997) Journal of the American Society for Mass Spectrometry , vol.8 , Issue.7 , pp. 681-687
    • Chen, Y.-L.1    Collings, B.A.2    Douglas, D.J.3
  • 34
    • 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
  • 35
    • 44049116161 scopus 로고
    • Collisional focusing effects in radio-frequency quadrupoles
    • Douglas, D. J., French, J. B.: Collisional Focusing Effects in Radio-Frequency 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
  • 36
    • 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
  • 37
    • 0031854618 scopus 로고    scopus 로고
    • Stability of a highly charged noncovalent complex in the gas phase: Holomyoglobin
    • DOI 10.1002/(SICI)1097-0231(19980815)12:15<1003::AID-RCM275>3.0. CO;2-#
    • Chen, Y. L., Campbell, J. M., Collings, B. A., Konermann, L., Douglas, D. J.: Stability of A Highly Charged Noncovalent Complex in the Gas Phase: Holomyoglobin. Rapid Commun. Mass Spectrom. 12, 1003-1010(1998) (Pubitemid 28351498)
    • (1998) Rapid Communications in Mass Spectrometry , vol.12 , Issue.15 , pp. 1003-1010
    • Chen, Y.-L.1    Campbell, J.M.2    Collings, B.A.3    Konermann, L.4    Douglas, D.J.5
  • 40
    • 34548768193 scopus 로고    scopus 로고
    • Symmetric behavior of hemoglobin α- and β- subunits during acid-induced denaturation observed by electrospray mass spectrometry
    • DOI 10.1021/bi701076q
    • 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) (Pubitemid 47421998)
    • (2007) Biochemistry , vol.46 , Issue.37 , pp. 10675-10684
    • Boys, B.L.1    Kuprowski, M.C.2    Konermann, L.3
  • 41
    • 0006739227 scopus 로고    scopus 로고
    • A spectrophotometric method for the simultaneous determination of myoglobin and hemoglobin in extracts of human muscle
    • Deduve, C.: A Spectrophotometric Method for the Simultaneous Determination of Myoglobin and Hemoglobin in Extracts of Human Muscle. Acta Chem. Scand. 2, 264-289(1998)
    • (1998) Acta Chem. Scand. , vol.2 , pp. 264-289
    • Deduve, C.1
  • 42
    • 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(1993)
    • (1993) Acta Chem. Scand. , vol.7 , pp. 1284-1287
    • Paul, K.G.1    Theorell, H.2    Akeson, A.3
  • 43
    • 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(1995)
    • (1995) Biochemistry , vol.4 , pp. 545-551
    • Antonini, E.1    Brunori, M.2    Wyman, J.3
  • 45
    • 34250748490 scopus 로고    scopus 로고
    • Analysis of Protein Mixtures by Electrospray Mass Spectrometry: Effects of Conformation and Desolvation Behavior on the Signal Intensities of Hemoglobin Subunits
    • DOI 10.1016/j.jasms.2007.04.002, PII S1044030507002942
    • Kuprowski, M. C., Boys, B. L., Konermann, L.: Analysis of Protein Mixtures by Electrospray Mass Spectrometry: Effects of Conformation and Desolvation Behavior on the Signal Intensities of Hemoglobin Subunits. J. Am. Soc. Mass Spectrom. 18, 1279-1285(2007) (Pubitemid 46963596)
    • (2007) Journal of the American Society for Mass Spectrometry , vol.18 , Issue.7 , pp. 1279-1285
    • Kuprowski, M.C.1    Boys, B.L.2    Konermann, L.3
  • 46
    • 0017073824 scopus 로고    scopus 로고
    • Carbamoylated hemoglobin - A and hemoglobin-S-physical properties
    • Williams, R. C., Kim, H.: Carbamoylated Hemoglobin-A and Hemoglobin-S - Physical Properties. Biochemistry 15, 2207-2211(1996)
    • (1996) Biochemistry , vol.15 , pp. 2207-2211
    • Williams, R.C.1    Kim, H.2
  • 48
    • 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(1990)
    • (1990) J. Biol. Chem. , vol.245 , pp. 5166-5168
    • Fish, W.W.1    Reynolds, J.A.2    Tanford, C.3
  • 49
    • 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(1990)
    • (1990) J. Biochem. , vol.68 , pp. 331-340
    • Ogasawar, N.1    Yoshino, M.2    Asai, J.P.3
  • 50
    • 0021260706 scopus 로고
    • Iodothyronines: Oxidative deiodination by hemoglobin and inhibition of lipid peroxidation
    • Tseng, Y. C. L., Latham, K. R.: Iodothyronines: Oxidative Deiodination by Hemoglobin and Inhibition of Lipid Peroxidation. Lipids 19, 96-102(1994)
    • (1994) Lipids , vol.19 , pp. 96-102
    • Tseng, Y.C.L.1    Latham, K.R.2
  • 51
    • 24644525124 scopus 로고    scopus 로고
    • Enhanced inhibition of polymerization of sickle cell hemoglobin in the presence of recombinant mutants of human fetal hemoglobin with substitutions at position 43 in the γ-chain
    • DOI 10.1021/bi050300z
    • Tam, M. F., Chen, J., Tam, T. C. S., Tsai, C. H., Shen, T. J., Simplaceanu, V., Feinstein, T. N., Barrick, D., Ho, C.: Enhanced Inhibition of Polymerization of Sickle Cell Hemoglobin in the Presence of Recombinant Mutants of Human Fetal Hemoglobin with Substitutions at Position 43 in the γ Chain. Biochemistry 44, 12188-12195(2005) (Pubitemid 41285717)
    • (2005) Biochemistry , vol.44 , Issue.36 , pp. 12188-12195
    • Tam, M.F.1    Chen, J.2    Tam, T.-C.S.3    Tsai, C.-H.4    Shen, T.-J.5    Simplaceanu, V.6    Feinstein, T.N.7    Barrick, D.8    Ho, C.9
  • 55
    • 31044438688 scopus 로고    scopus 로고
    • Coulomb effects in binding of heme in gas-phase ions of myoglobin
    • DOI 10.1002/rcm.2273
    • Mark, K. J., Douglas, D. J.: Coulomb Effects in Binding of Heme in Gas-Phase Ions of Myoglobin. Rapid Commun. Mass Spectrom. 20, 111-117(2006) (Pubitemid 43121609)
    • (2006) Rapid Communications in Mass Spectrometry , vol.20 , Issue.2 , pp. 111-117
    • Mark, K.J.1    Douglas, D.J.2
  • 56
    • 0035564266 scopus 로고    scopus 로고
    • Metastable ion formation and disparate charge separation in the gas-phase dissection of protein assemblies studied by orthogonal time-of-flight mass spectrometry
    • DOI 10.1016/S1044-0305(00)00227-0, PII S1044030500002270
    • Versluis, C., van der Staaij, A., Stokvis, E., Heck, A. J. R., de Craene, B.: Metastable Ion Formation and Disparate Charge Separation in the Gas-Phase Dissection of Protein Assemblies Studied by Orthogonal Time-of-Flight Mass Spectrometry. J. Am. Soc. Mass Spectrom. 12, 329-336(2001) (Pubitemid 34546627)
    • (2001) Journal of the American Society for Mass Spectrometry , vol.12 , Issue.3 , pp. 329-336
    • Versluis, C.1    Van Der Staaij, A.2    Stokvis, E.3    Heck, A.J.R.4    De Craene, B.5
  • 57
    • 4744373182 scopus 로고    scopus 로고
    • Further studies on the origins of asymmetric charge partitioning in protein homodimers
    • DOI 10.1016/j.jasms.2004.06.006, PII S1044030504003861
    • Jurchen, J. C., Garcia, D. E., Williams, E. R.: Further Studies on the Origins of Asymmetric Charge Partitioning in Protein Homodimers. J. Am. Soc. Mass Spectrom. 15, 1408-1415(2004) (Pubitemid 39311691)
    • (2004) Journal of the American Society for Mass Spectrometry , vol.15 , Issue.10 , pp. 1408-1415
    • Jurchen, J.C.1    Garcia, D.E.2    Williams, E.R.3
  • 58
    • 0037420384 scopus 로고    scopus 로고
    • Origin of asymmetric charge partitioning in the dissociation of gas-phase protein homodimers
    • DOI 10.1021/ja0211508
    • Jurchen, J. C., Williams, E. R.: Origin of Asymmetric Charge Partitioning in the Dissociation of Gas-phase Protein Homodimers. J. Am. Chem. Soc. 125, 2817-2826(2003) (Pubitemid 36512268)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.9 , pp. 2817-2826
    • Jurchen, J.C.1    Williams, E.R.2
  • 59
    • 36349018185 scopus 로고    scopus 로고
    • Theoretical Investigations of the Dissociation of Charged Protein Complexes in the Gas Phase
    • DOI 10.1016/j.jasms.2007.09.022, PII S1044030507008665
    • Wanasundara, S. N., Thachuk, M.: Theoretical Investigations of the Dissociation of Charged Protein Complexes in the Gas Phase. J. Am. Soc. Mass Spectrom. 18, 2242-2253(2007) (Pubitemid 350161339)
    • (2007) Journal of the American Society for Mass Spectrometry , vol.18 , Issue.12 , pp. 2242-2253
    • Wanasundara, S.N.1    Thachuk, M.2
  • 60
    • 33845951972 scopus 로고    scopus 로고
    • Gas Phase Noncovalent Protein Complexes that Retain Solution Binding Properties: Binding of Xylobiose Inhibitors to the β-1, 4 Exoglucanase from Cellulomonas fimi
    • DOI 10.1016/j.jasms.2006.08.012, PII S104403050600777X
    • Tesic, M., Wicki, J., Poon, D. K. Y., Withers, S. G., Douglas, D. J.: Gas Phase Noncovalent Protein Complexes that Retain Solution Binding Properties: Binding of Xylobiose Inhibitors to the β-1, 4 Exoglucanase from Cellulomonas fimi. J. Am. Soc. Mass Spectrom. 18, 64-73(2007) (Pubitemid 46038164)
    • (2007) Journal of the American Society for Mass Spectrometry , vol.18 , Issue.1 , pp. 64-73
    • Tesic, M.1    Wicki, J.2    Poon, D.K.Y.3    Withers, S.G.4    Douglas, D.J.5
  • 61
    • 0034725040 scopus 로고    scopus 로고
    • Assembly of γ- with α-globin chains to form human fetal hemoglobin in vitro and in vivo
    • DOI 10.1074/jbc.C000137200
    • Adachi, K., Zhao, Y., Yamaguchi, T., Surrey, S.: Assembly of γ-with α-Globin Chains to Form Human Fetal Hemoglobin in Vitro and in Vivo. J. Biol. Chem. 275, 12424-12429(2000) (Pubitemid 30241383)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.17 , pp. 12424-12429
    • Adachi, K.1    Zhao, Y.2    Yamaguchi, T.3    Surrey, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.