메뉴 건너뛰기




Volumn 27, Issue 1, 2012, Pages 32-39

Enhanced nitrite reductase activity associated with the haptoglobin complexed hemoglobin dimer: Functional and antioxidative implications

Author keywords

Haptoglobin; Hemoglobin; Nitrite reductase

Indexed keywords

DIMER; HAPTOGLOBIN; HEMOGLOBIN; HEMOGLOBIN DIMER; NITRIC OXIDE; NITRITE REDUCTASE; OXYGEN; UNCLASSIFIED DRUG;

EID: 84861634126     PISSN: 10898603     EISSN: 10898611     Source Type: Journal    
DOI: 10.1016/j.niox.2012.04.002     Document Type: Article
Times cited : (16)

References (68)
  • 1
    • 77953353898 scopus 로고    scopus 로고
    • Setbacks in blood substitutes research and development: A biochemical perspective
    • A.I. Alayash Setbacks in blood substitutes research and development: a biochemical perspective Clin. Lab. Med. 30 2010 381 389
    • (2010) Clin. Lab. Med. , vol.30 , pp. 381-389
    • Alayash, A.I.1
  • 2
    • 58849143962 scopus 로고    scopus 로고
    • Radical producing and consuming reactions of hemoglobin: How can we limit toxicity?
    • C.E. Cooper Radical producing and consuming reactions of hemoglobin: how can we limit toxicity? Artif. Organs 33 2009 110 114
    • (2009) Artif. Organs , vol.33 , pp. 110-114
    • Cooper, C.E.1
  • 5
    • 15944398355 scopus 로고    scopus 로고
    • The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin: A novel mechanism of human disease
    • R. Rother, L. Bell, P. Hillmen, and M. Gladwin The clinical sequelae of intravascular hemolysis and extracellular plasma hemoglobin: a novel mechanism of human disease JAMA 293 2005 1653 1662
    • (2005) JAMA , vol.293 , pp. 1653-1662
    • Rother, R.1    Bell, L.2    Hillmen, P.3    Gladwin, M.4
  • 6
    • 0037054809 scopus 로고    scopus 로고
    • Myoglobin as a model system for designing heme protein based blood substitutes
    • Y. Dou, D. Maillett, R. Eich, and J. Olson Myoglobin as a model system for designing heme protein based blood substitutes Biophys. Chem. 98 2002 127 148
    • (2002) Biophys. Chem. , vol.98 , pp. 127-148
    • Dou, Y.1    Maillett, D.2    Eich, R.3    Olson, J.4
  • 7
    • 1242353138 scopus 로고    scopus 로고
    • Oxygen therapeutics: Can we tame haemoglobin?
    • A.I. Alayash Oxygen therapeutics: can we tame haemoglobin? Nat. Rev. Drug Discov. 3 2004 152 159
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 152-159
    • Alayash, A.I.1
  • 8
    • 79551477079 scopus 로고    scopus 로고
    • Haptoglobin: Old protein with new functions
    • A.I. Alayash Haptoglobin: old protein with new functions Clin. Chim. Acta 412 2011 493 498
    • (2011) Clin. Chim. Acta , vol.412 , pp. 493-498
    • Alayash, A.I.1
  • 9
    • 77949507206 scopus 로고    scopus 로고
    • Clearance and control mechanisms of hemoglobin from cradle to grave
    • D.J. Schaer, and A.I. Alayash Clearance and control mechanisms of hemoglobin from cradle to grave Antioxid. Redox Signal. 12 2010 181 184
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 181-184
    • Schaer, D.J.1    Alayash, A.I.2
  • 10
    • 77957331298 scopus 로고    scopus 로고
    • Hemoglobin-based oxygen carriers: From mechanisms of toxicity and clearance to rational drug design
    • P.W. Buehler, F. D'Agnillo, and D.J. Schaer Hemoglobin-based oxygen carriers: from mechanisms of toxicity and clearance to rational drug design Trends Mol. Med. 16 2010 447 457
    • (2010) Trends Mol. Med. , vol.16 , pp. 447-457
    • Buehler, P.W.1    D'Agnillo, F.2    Schaer, D.J.3
  • 11
    • 77949497125 scopus 로고    scopus 로고
    • Evolutionary aspects of hemoglobin scavengers
    • K.B. Wicher, and E. Fries Evolutionary aspects of hemoglobin scavengers Antioxid. Redox Signal. 12 2010 249 259
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 249-259
    • Wicher, K.B.1    Fries, E.2
  • 13
    • 0014959633 scopus 로고
    • Studies on the reaction of haptoglobin with hemoglobin and hemoglobin chains. 3. Observations on the kinetics of the reaction of the haptoglobin-hemoglobin complexes with carbon monoxide
    • A. Alfsen, E. Chiancone, E. Antonini, M. Waks, and J. Wyman Studies on the reaction of haptoglobin with hemoglobin and hemoglobin chains. 3. Observations on the kinetics of the reaction of the haptoglobin-hemoglobin complexes with carbon monoxide Biochim. Biophys. Acta 207 1970 395 403
    • (1970) Biochim. Biophys. Acta , vol.207 , pp. 395-403
    • Alfsen, A.1    Chiancone, E.2    Antonini, E.3    Waks, M.4    Wyman, J.5
  • 14
    • 0015618830 scopus 로고
    • Kinetics of the reaction between oxygen and haemoglobin bound to haptoglobin
    • E. Chiancone, E. Antonini, M. Brunori, A. Alfsen, and F. Lavialle Kinetics of the reaction between oxygen and haemoglobin bound to haptoglobin Biochem. J. 133 1973 205 207
    • (1973) Biochem. J. , vol.133 , pp. 205-207
    • Chiancone, E.1    Antonini, E.2    Brunori, M.3    Alfsen, A.4    Lavialle, F.5
  • 15
    • 0014030856 scopus 로고
    • Kinetics of the reaction of carbon monoxide with the hemoglobin- haptoglobin complex
    • R.L. Nagel, and Q.H. Gibson Kinetics of the reaction of carbon monoxide with the hemoglobin-haptoglobin complex J. Mol. Biol. 22 1966 249 255
    • (1966) J. Mol. Biol. , vol.22 , pp. 249-255
    • Nagel, R.L.1    Gibson, Q.H.2
  • 17
    • 0037110570 scopus 로고    scopus 로고
    • Allosteric effects of chloride ions at the intradimeric alpha1beta1 and alpha2beta2 interfaces of human hemoglobin
    • I.N. Rujan, and I.M. Russu Allosteric effects of chloride ions at the intradimeric alpha1beta1 and alpha2beta2 interfaces of human hemoglobin Proteins 49 2002 413 419
    • (2002) Proteins , vol.49 , pp. 413-419
    • Rujan, I.N.1    Russu, I.M.2
  • 19
    • 0033528707 scopus 로고    scopus 로고
    • The conformational and dynamic basis for ligand binding reactivity in hemoglobin Ypsilanti (beta 99 asp->Tyr): Origin of the quaternary enhancement effect
    • J. Huang, L.J. Juszczak, E.S. Peterson, C.F. Shannon, M. Yang, S. Huang, G.V. Vidugiris, and J.M. Friedman The conformational and dynamic basis for ligand binding reactivity in hemoglobin Ypsilanti (beta 99 asp->Tyr): origin of the quaternary enhancement effect Biochemistry 38 1999 4514 4525
    • (1999) Biochemistry , vol.38 , pp. 4514-4525
    • Huang, J.1    Juszczak, L.J.2    Peterson, E.S.3    Shannon, C.F.4    Yang, M.5    Huang, S.6    Vidugiris, G.V.7    Friedman, J.M.8
  • 20
    • 0032584258 scopus 로고    scopus 로고
    • Preparation and kinetic characterization of a series of betaW37 variants of human hemoglobin A: Evidence for high-affinity T quaternary structures
    • L.D. Kwiatkowski, H.L. Hui, A. Wierzba, R.W. Noble, R.Y. Walder, E.S. Peterson, S.G. Sligar, and K.E. Sanders Preparation and kinetic characterization of a series of betaW37 variants of human hemoglobin A: evidence for high-affinity T quaternary structures Biochemistry 37 1998 4325 4335
    • (1998) Biochemistry , vol.37 , pp. 4325-4335
    • Kwiatkowski, L.D.1    Hui, H.L.2    Wierzba, A.3    Noble, R.W.4    Walder, R.Y.5    Peterson, E.S.6    Sligar, S.G.7    Sanders, K.E.8
  • 21
    • 0030888912 scopus 로고    scopus 로고
    • 2 binding and subunit assembly in human hemoglobin: Titration of the quaternary enhancement effect
    • 2 binding and subunit assembly in human hemoglobin: titration of the quaternary enhancement effect Biophys. Chem. 64 1997 271 287
    • (1997) Biophys. Chem. , vol.64 , pp. 271-287
    • Doyle, M.L.1    Holt, J.M.2    Ackers, G.K.3
  • 22
    • 0030671072 scopus 로고    scopus 로고
    • Kinetic hole burning, hole filling, and conformational relaxation in heme proteins: Direct evidence for the functional significance of a hierarchy of dynamical processes
    • J. Huang, A. Ridsdale, J. Wang, and J.M. Friedman Kinetic hole burning, hole filling, and conformational relaxation in heme proteins: direct evidence for the functional significance of a hierarchy of dynamical processes Biochemistry 36 1997 14353 14365
    • (1997) Biochemistry , vol.36 , pp. 14353-14365
    • Huang, J.1    Ridsdale, A.2    Wang, J.3    Friedman, J.M.4
  • 23
    • 0026496538 scopus 로고
    • Cooperative oxygen binding, subunit assembly, and sulfhydryl reaction kinetics of the eight cyanomet intermediate ligation states of human hemoglobin
    • M.L. Doyle, and G.K. Ackers Cooperative oxygen binding, subunit assembly, and sulfhydryl reaction kinetics of the eight cyanomet intermediate ligation states of human hemoglobin Biochemistry 31 1992 11182 11195
    • (1992) Biochemistry , vol.31 , pp. 11182-11195
    • Doyle, M.L.1    Ackers, G.K.2
  • 24
    • 0008530152 scopus 로고
    • Quaternary enhancement in binding of oxygen by human hemoglobin
    • F.C. Mills, and G.K. Ackers Quaternary enhancement in binding of oxygen by human hemoglobin Proc. Natl Acad. Sci. USA 76 1979 273 277
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 273-277
    • Mills, F.C.1    Ackers, G.K.2
  • 26
    • 23644459872 scopus 로고    scopus 로고
    • The reaction between nitrite and deoxyhemoglobin. Reassessment of reaction kinetics and stoichiometry
    • K.T. Huang, A. Keszler, N. Patel, R.P. Patel, M.T. Gladwin, D.B. Kim-Shapiro, and N. Hogg The reaction between nitrite and deoxyhemoglobin. Reassessment of reaction kinetics and stoichiometry J. Biol. Chem. 280 2005 31126 31131
    • (2005) J. Biol. Chem. , vol.280 , pp. 31126-31131
    • Huang, K.T.1    Keszler, A.2    Patel, N.3    Patel, R.P.4    Gladwin, M.T.5    Kim-Shapiro, D.B.6    Hogg, N.7
  • 28
    • 33846027866 scopus 로고    scopus 로고
    • Nitrite reductase activity of sol-gel-encapsulated deoxyhemoglobin. Influence of quaternary and tertiary structure
    • C.J. Roche, D. Dantsker, U. Samuni, and J.M. Friedman Nitrite reductase activity of sol-gel-encapsulated deoxyhemoglobin. Influence of quaternary and tertiary structure J. Biol. Chem. 281 2006 36874 36882
    • (2006) J. Biol. Chem. , vol.281 , pp. 36874-36882
    • Roche, C.J.1    Dantsker, D.2    Samuni, U.3    Friedman, J.M.4
  • 29
    • 79959535344 scopus 로고    scopus 로고
    • Structural and functional studies indicating altered redox properties of hemoglobin E: IMPLICATIONS for PRODUCTION of BIOACTIVE NITRIC OXIDE
    • C.J. Roche, V. Malashkevich, T.C. Balazs, D. Dantsker, Q. Chen, J. Moreira, S.C. Almo, J.M. Friedman, and R.E. Hirsch Structural and functional studies indicating altered redox properties of hemoglobin E: IMPLICATIONS FOR PRODUCTION OF BIOACTIVE NITRIC OXIDE J. Biol. Chem. 286 2011 23452 23466
    • (2011) J. Biol. Chem. , vol.286 , pp. 23452-23466
    • Roche, C.J.1    Malashkevich, V.2    Balazs, T.C.3    Dantsker, D.4    Chen, Q.5    Moreira, J.6    Almo, S.C.7    Friedman, J.M.8    Hirsch, R.E.9
  • 31
    • 62249186925 scopus 로고    scopus 로고
    • Pegylated hemoglobins mechanisms to avoid vasoconstriction and maintain perfusion
    • P. Cabrales, and J. Friedman Pegylated hemoglobins mechanisms to avoid vasoconstriction and maintain perfusion Transfus. Altern. Transfus. Med. 9 2007 281 293
    • (2007) Transfus. Altern. Transfus. Med. , vol.9 , pp. 281-293
    • Cabrales, P.1    Friedman, J.2
  • 32
    • 53249134617 scopus 로고    scopus 로고
    • Polyethylene glycol conjugation enhances the nitrite reductase activity of native and cross-linked hemoglobin
    • F.E. Lui, P. Dong, and R. Kluger Polyethylene glycol conjugation enhances the nitrite reductase activity of native and cross-linked hemoglobin Biochemistry 47 2008 10773 10780
    • (2008) Biochemistry , vol.47 , pp. 10773-10780
    • Lui, F.E.1    Dong, P.2    Kluger, R.3
  • 33
    • 33751198276 scopus 로고    scopus 로고
    • Dissociation of local nitric oxide concentration and vasoconstriction in the presence of cell-free hemoglobin oxygen carriers
    • A.G. Tsai, P. Cabrales, B.N. Manjula, S.A. Acharya, R.M. Winslow, and M. Intaglietta Dissociation of local nitric oxide concentration and vasoconstriction in the presence of cell-free hemoglobin oxygen carriers Blood 108 2006 3603 3610
    • (2006) Blood , vol.108 , pp. 3603-3610
    • Tsai, A.G.1    Cabrales, P.2    Manjula, B.N.3    Acharya, S.A.4    Winslow, R.M.5    Intaglietta, M.6
  • 35
    • 4344592222 scopus 로고    scopus 로고
    • MP4, a new nonvasoactive polyethylene glycol-hemoglobin conjugate
    • R.M. Winslow MP4, a new nonvasoactive polyethylene glycol-hemoglobin conjugate Artif. Organs 28 2004 800 806
    • (2004) Artif. Organs , vol.28 , pp. 800-806
    • Winslow, R.M.1
  • 37
    • 0016258287 scopus 로고
    • Influence of globin structure on the state of the heme I Human deoxyhemoglobin
    • M.F. Perutz, J.E. Ladner, S.R. Simon, and C. Ho Influence of globin structure on the state of the heme I Human deoxyhemoglobin Biochemistry 13 1974 2163 2173
    • (1974) Biochemistry , vol.13 , pp. 2163-2173
    • Perutz, M.F.1    Ladner, J.E.2    Simon, S.R.3    Ho, C.4
  • 39
    • 0028969604 scopus 로고
    • Correlation of carbon monoxide association rates and the position of absorption band III in hemoproteins
    • L. Kiger, F. Stetzkowski-Marden, C. Poyart, and M.C. Marden Correlation of carbon monoxide association rates and the position of absorption band III in hemoproteins Eur. J. Biochem. 228 1995 665 668
    • (1995) Eur. J. Biochem. , vol.228 , pp. 665-668
    • Kiger, L.1    Stetzkowski-Marden, F.2    Poyart, C.3    Marden, M.C.4
  • 40
    • 0023236885 scopus 로고
    • Time dependence of near-infrared spectra of photodissociated hemoglobin and myoglobin
    • M. Sassaroli, and D.L. Rousseau Time dependence of near-infrared spectra of photodissociated hemoglobin and myoglobin Biochemistry 26 1987 3092 3098
    • (1987) Biochemistry , vol.26 , pp. 3092-3098
    • Sassaroli, M.1    Rousseau, D.L.2
  • 41
    • 85044562599 scopus 로고
    • Structural and functional significance of inhomogeneous line broadening of band III in hemoglobin and Fe-Mn hybrid hemoglobins
    • M.D. Chavez, S.H. Courtney, M.R. Chance, D. Kuila, J. Nocek, B.M. Hoffman, J.M. Friedman, and M.R. Ondrias Structural and functional significance of inhomogeneous line broadening of band III in hemoglobin and Fe-Mn hybrid hemoglobins Biochemistry 29 1990 4844 4852
    • (1990) Biochemistry , vol.29 , pp. 4844-4852
    • Chavez, M.D.1    Courtney, S.H.2    Chance, M.R.3    Kuila, D.4    Nocek, J.5    Hoffman, B.M.6    Friedman, J.M.7    Ondrias, M.R.8
  • 42
    • 15544363535 scopus 로고    scopus 로고
    • Spectroscopic markers of the T<->R quaternary transition in human hemoglobin
    • G. Schiro, M. Cammarata, M. Levantino, and A. Cupane Spectroscopic markers of the T<->R quaternary transition in human hemoglobin Biophys. Chem. 114 2005 27 33
    • (2005) Biophys. Chem. , vol.114 , pp. 27-33
    • Schiro, G.1    Cammarata, M.2    Levantino, M.3    Cupane, A.4
  • 43
    • 0001257259 scopus 로고
    • Transient and cryogenic studies of photodissociated hemoglobin and myoglobin
    • T.G. Spiro, John Wiley & Sons New York
    • D.L. Rousseau, and J.M. Friedman Transient and cryogenic studies of photodissociated hemoglobin and myoglobin T.G. Spiro, Biological Applications of Raman Spectroscopy 1988 John Wiley & Sons New York 133 215
    • (1988) Biological Applications of Raman Spectroscopy , pp. 133-215
    • Rousseau, D.L.1    Friedman, J.M.2
  • 44
    • 35348847304 scopus 로고    scopus 로고
    • Quaternary relaxations in sol-gel encapsulated hemoglobin studied via NIR and UV spectroscopy
    • G. Schiro, and A. Cupane Quaternary relaxations in sol-gel encapsulated hemoglobin studied via NIR and UV spectroscopy Biochemistry 46 2007 11568 11576
    • (2007) Biochemistry , vol.46 , pp. 11568-11576
    • Schiro, G.1    Cupane, A.2
  • 45
    • 0026333178 scopus 로고
    • Involvement of the distal histidine in the low affinity exhibited by Hb Chico (Lys beta 66 - -Thr) and its isolated beta chains
    • C. Bonaventura, R. Cashon, J. Bonaventura, M. Perutz, G. Fermi, and D.T. Shih Involvement of the distal histidine in the low affinity exhibited by Hb Chico (Lys beta 66 - -Thr) and its isolated beta chains J. Biol. Chem. 266 1991 23033 23040
    • (1991) J. Biol. Chem. , vol.266 , pp. 23033-23040
    • Bonaventura, C.1    Cashon, R.2    Bonaventura, J.3    Perutz, M.4    Fermi, G.5    Shih, D.T.6
  • 47
    • 0033621891 scopus 로고    scopus 로고
    • Cys-93-betabeta-succinimidophenyl polyethylene glycol, hemoglobin A. Intramolecular cross-bridging of hemoglobin outside the central cavity
    • B.N. Manjula, A. Malavalli, P.K. Smith, N.L. Chan, A. Arnone, J.M. Friedman, and A.S. Acharya Cys-93-betabeta-succinimidophenyl polyethylene glycol, hemoglobin A. Intramolecular cross-bridging of hemoglobin outside the central cavity J. Biol. Chem. 275 2000 2000 5527 5534
    • (2000) J. Biol. Chem. , vol.275 , Issue.2000 , pp. 5527-5534
    • Manjula, B.N.1    Malavalli, A.2    Smith, P.K.3    Chan, N.L.4    Arnone, A.5    Friedman, J.M.6    Acharya, A.S.7
  • 48
    • 33846969212 scopus 로고    scopus 로고
    • Influence of intramolecular cross-links on the molecular, structural and functional properties of PEGylated haemoglobin
    • T. Hu, B.N. Manjula, D. Li, M. Brenowitz, and S.A. Acharya Influence of intramolecular cross-links on the molecular, structural and functional properties of PEGylated haemoglobin Biochem. J. 402 2007 143 151
    • (2007) Biochem. J. , vol.402 , pp. 143-151
    • Hu, T.1    Manjula, B.N.2    Li, D.3    Brenowitz, M.4    Acharya, S.A.5
  • 49
    • 72449130852 scopus 로고    scopus 로고
    • Enhancing nitrite reductase activity of modified hemoglobin: Bis-tetramers and their PEGylated derivatives
    • F.E. Lui, and R. Kluger Enhancing nitrite reductase activity of modified hemoglobin: bis-tetramers and their PEGylated derivatives Biochemistry 48 2009 11912 11919
    • (2009) Biochemistry , vol.48 , pp. 11912-11919
    • Lui, F.E.1    Kluger, R.2
  • 50
    • 2942568125 scopus 로고    scopus 로고
    • Oxygen binding and oxidation reactions of human hemoglobin conjugated to carboxylate dextran
    • Y. Jia, F. Wood, P. Menu, B. Faivre, A. Caron, and A.I. Alayash Oxygen binding and oxidation reactions of human hemoglobin conjugated to carboxylate dextran Biochim. Biophys. Acta 1672 2004 164 173
    • (2004) Biochim. Biophys. Acta , vol.1672 , pp. 164-173
    • Jia, Y.1    Wood, F.2    Menu, P.3    Faivre, B.4    Caron, A.5    Alayash, A.I.6
  • 52
    • 7244239027 scopus 로고    scopus 로고
    • Spectroscopic and functional characterization of T state hemoglobin conformations encapsulated in silica gels
    • U. Samuni, D. Dantsker, L.J. Juszczak, S. Bettati, L. Ronda, A. Mozzarelli, and J.M. Friedman Spectroscopic and functional characterization of T state hemoglobin conformations encapsulated in silica gels Biochemistry 43 2004 13674 13682
    • (2004) Biochemistry , vol.43 , pp. 13674-13682
    • Samuni, U.1    Dantsker, D.2    Juszczak, L.J.3    Bettati, S.4    Ronda, L.5    Mozzarelli, A.6    Friedman, J.M.7
  • 53
    • 35548949877 scopus 로고    scopus 로고
    • Conformational dependence of hemoglobin reactivity under high viscosity conditions: The role of solvent slaved dynamics
    • U. Samuni, C.J. Roche, D. Dantsker, and J.M. Friedman Conformational dependence of hemoglobin reactivity under high viscosity conditions: the role of solvent slaved dynamics J. Am. Chem. Soc. 129 2007 12756 12764
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 12756-12764
    • Samuni, U.1    Roche, C.J.2    Dantsker, D.3    Friedman, J.M.4
  • 54
    • 33644680949 scopus 로고    scopus 로고
    • Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: The combined use of mutagenesis and sol-gel encapsulation
    • U. Samuni, C.J. Roche, D. Dantsker, L.J. Juszczak, and J.M. Friedman Modulation of reactivity and conformation within the T-quaternary state of human hemoglobin: the combined use of mutagenesis and sol-gel encapsulation Biochemistry 45 2006 2820 2835
    • (2006) Biochemistry , vol.45 , pp. 2820-2835
    • Samuni, U.1    Roche, C.J.2    Dantsker, D.3    Juszczak, L.J.4    Friedman, J.M.5
  • 55
    • 44449098314 scopus 로고    scopus 로고
    • Kinetics of reaction of nitrite with deoxy hemoglobin after rapid deoxygenation or predeoxygenation by dithionite measured in solution and bound to the cytoplasmic domain of band 3 (SLC4A1)
    • J.M. Salhany Kinetics of reaction of nitrite with deoxy hemoglobin after rapid deoxygenation or predeoxygenation by dithionite measured in solution and bound to the cytoplasmic domain of band 3 (SLC4A1) Biochemistry 47 2008 6059 6072
    • (2008) Biochemistry , vol.47 , pp. 6059-6072
    • Salhany, J.M.1
  • 56
    • 41249092640 scopus 로고    scopus 로고
    • Nitrite reductase activity of hemoglobin S (sickle) provides insight into contributions of heme redox potential versus ligand affinity
    • R. Grubina, S. Basu, M. Tiso, D.B. Kim-Shapiro, and M.T. Gladwin Nitrite reductase activity of hemoglobin S (sickle) provides insight into contributions of heme redox potential versus ligand affinity J. Biol. Chem. 283 2008 3628 3638
    • (2008) J. Biol. Chem. , vol.283 , pp. 3628-3638
    • Grubina, R.1    Basu, S.2    Tiso, M.3    Kim-Shapiro, D.B.4    Gladwin, M.T.5
  • 58
    • 1942502768 scopus 로고    scopus 로고
    • Domain-specific effector interactions within the central cavity of human adult hemoglobin in solution and in porous sol-gel matrices: Evidence for long-range communication pathways
    • E.S. Peterson, R. Shinder, I. Khan, L. Juczszak, J. Wang, B. Manjula, S.A. Acharya, C. Bonaventura, and J.M. Friedman Domain-specific effector interactions within the central cavity of human adult hemoglobin in solution and in porous sol-gel matrices: evidence for long-range communication pathways Biochemistry 43 2004 4832 4843
    • (2004) Biochemistry , vol.43 , pp. 4832-4843
    • Peterson, E.S.1    Shinder, R.2    Khan, I.3    Juczszak, L.4    Wang, J.5    Manjula, B.6    Acharya, S.A.7    Bonaventura, C.8    Friedman, J.M.9
  • 60
    • 0013818097 scopus 로고
    • Comparative haptoglobin binding properties of oxyhemoglobin and deoxyhemoglobin
    • R.L. Nagel, M.C. Rothman, T.B. Bradley Jr., and H.M. Ranney Comparative haptoglobin binding properties of oxyhemoglobin and deoxyhemoglobin J. Biol. Chem. 240 1965 4543 4545
    • (1965) J. Biol. Chem. , vol.240 , pp. 4543-4545
    • Nagel, R.L.1    Rothman, M.C.2    Bradley Jr., T.B.3    Ranney, H.M.4
  • 61
    • 0026795182 scopus 로고
    • A third quaternary structure of human hemoglobin A at 1.7-A resolution
    • M.M. Silva, P.H. Rogers, and A. Arnone A third quaternary structure of human hemoglobin A at 1.7-A resolution J. Biol. Chem. 267 1992 17248 17256
    • (1992) J. Biol. Chem. , vol.267 , pp. 17248-17256
    • Silva, M.M.1    Rogers, P.H.2    Arnone, A.3
  • 62
    • 0034687668 scopus 로고    scopus 로고
    • Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin
    • T.C. Mueser, P.H. Rogers, and A. Arnone Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin Biochemistry 39 2000 15353 15364
    • (2000) Biochemistry , vol.39 , pp. 15353-15364
    • Mueser, T.C.1    Rogers, P.H.2    Arnone, A.3
  • 66
    • 79955111921 scopus 로고    scopus 로고
    • Exogenous nitric oxide prevents cardiovascular collapse during hemorrhagic shock
    • P. Nachuraju, A.J. Friedman, J.M. Friedman, and P. Cabrales Exogenous nitric oxide prevents cardiovascular collapse during hemorrhagic shock Resuscitation 82 2011 607 613
    • (2011) Resuscitation , vol.82 , pp. 607-613
    • Nachuraju, P.1    Friedman, A.J.2    Friedman, J.M.3    Cabrales, P.4
  • 67
    • 77955437788 scopus 로고    scopus 로고
    • Quantitative mass spectrometry defines an oxidative hotspot in hemoglobin that is specifically protected by haptoglobin
    • T. Pimenova, C.P. Pereira, P. Gehrig, P.W. Buehler, D.J. Schaer, and R. Zenobi Quantitative mass spectrometry defines an oxidative hotspot in hemoglobin that is specifically protected by haptoglobin J. Proteome Res. 9 2010 4061 4070
    • (2010) J. Proteome Res. , vol.9 , pp. 4061-4070
    • Pimenova, T.1    Pereira, C.P.2    Gehrig, P.3    Buehler, P.W.4    Schaer, D.J.5    Zenobi, R.6
  • 68
    • 79551477079 scopus 로고    scopus 로고
    • Haptoglobin: Old protein with new functions
    • A.I. Alayash Haptoglobin: old protein with new functions Clin. Chim. Acta 412 2011 493 498
    • (2011) Clin. Chim. Acta , vol.412 , pp. 493-498
    • Alayash, A.I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.