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Volumn 48, Issue 3, 2009, Pages 608-616

PEGylation of Val-1(α) destabilizes the tetrameric structure of hemoglobin

Author keywords

[No Author keywords available]

Indexed keywords

DISSOCIATION; HEMOGLOBIN;

EID: 59249106690     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801880y     Document Type: Article
Times cited : (30)

References (45)
  • 1
    • 0034214350 scopus 로고    scopus 로고
    • The prospects for red-cell substitutes
    • Klein, H. G. (2000) The prospects for red-cell substitutes. New Engl. J. Med. 342, 1666-1668.
    • (2000) New Engl. J. Med , vol.342 , pp. 1666-1668
    • Klein, H.G.1
  • 3
    • 33749234394 scopus 로고    scopus 로고
    • Extension arm facilitated PEGylation of proteins: Correlation of the structure of PEGylated Hemoglobin with the extent of PEGylation
    • Li, D., Manjula, B. N., and Acharya, A. S. (2006) Extension arm facilitated PEGylation of proteins: correlation of the structure of PEGylated Hemoglobin with the extent of PEGylation. Protein J. 25, 263-274.
    • (2006) Protein J , vol.25 , pp. 263-274
    • Li, D.1    Manjula, B.N.2    Acharya, A.S.3
  • 4
    • 23844456246 scopus 로고    scopus 로고
    • Conjugation of multiple copies of polyethylene glycol to hemoglobin facilitated through thiolation: Influence on hemoglobin structure and function
    • Manjula, B. N., Tsai, A. G., Intaglietta, M., Tsai, C-H., Ho, C., Smith, P. K., Perumalsamy, K., Kanika, N. D., Friedman, J. M., and Acharya, A. S. (2005) Conjugation of multiple copies of polyethylene glycol to hemoglobin facilitated through thiolation: Influence on hemoglobin structure and function. Protein J. 42, 133-146.
    • (2005) Protein J , vol.42 , pp. 133-146
    • Manjula, B.N.1    Tsai, A.G.2    Intaglietta, M.3    Tsai, C.-H.4    Ho, C.5    Smith, P.K.6    Perumalsamy, K.7    Kanika, N.D.8    Friedman, J.M.9    Acharya, A.S.10
  • 6
    • 0028167109 scopus 로고
    • Evidence of hemoglobin dissociation
    • Lunelli, L., Zuliani, P., and Baldini, G. (1994) Evidence of hemoglobin dissociation. Biopolymers 34, 747-757.
    • (1994) Biopolymers , vol.34 , pp. 747-757
    • Lunelli, L.1    Zuliani, P.2    Baldini, G.3
  • 7
    • 0343852150 scopus 로고    scopus 로고
    • Current status of artificial oxygen carriers
    • Spahn, D. R. (2000) Current status of artificial oxygen carriers. Adv. Drug Delivery Rev. 40, 143-151.
    • (2000) Adv. Drug Delivery Rev , vol.40 , pp. 143-151
    • Spahn, D.R.1
  • 8
    • 33846969212 scopus 로고    scopus 로고
    • Influence of intramolecular cross-links on the molecular, structural and functional properties of PEGylated hemoglobin
    • Hu, T., Manjula, B. N., Li, D., Brenowitz, M., and Acharya, S. A. (2007) Influence of intramolecular cross-links on the molecular, structural and functional properties of PEGylated hemoglobin. Biochem. J. 402, 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
  • 9
    • 29644434820 scopus 로고    scopus 로고
    • Influence of the chemistry of conjugation of poly(ethylene glycol) to Hb on the oxygen-binding and solution properties of the PEGHb conjugate
    • Hu, T., Prabhkaran, M., Acharya, S. A., and Manjula, B. N. (2005) Influence of the chemistry of conjugation of poly(ethylene glycol) to Hb on the oxygen-binding and solution properties of the PEGHb conjugate. Biochem. J. 392, 555-564.
    • (2005) Biochem. J , vol.392 , pp. 555-564
    • Hu, T.1    Prabhkaran, M.2    Acharya, S.A.3    Manjula, B.N.4
  • 12
    • 0018572809 scopus 로고
    • X-ray diffraction and solution studies of specifically carbamylated human hemoglobin A. Evidence for the location of a proton- and oxygen-linked chloride binding site at valine 1 alpha
    • O'Donnell, S., Mandaro, R., Schuster, T. M., and Arnone, A. (1979) X-ray diffraction and solution studies of specifically carbamylated human hemoglobin A. Evidence for the location of a proton- and oxygen-linked chloride binding site at valine 1 alpha. J. Biol. Chem. 254, 12204-12208.
    • (1979) J. Biol. Chem , vol.254 , pp. 12204-12208
    • O'Donnell, S.1    Mandaro, R.2    Schuster, T.M.3    Arnone, A.4
  • 13
    • 0020626848 scopus 로고
    • Selective carboxymethylation of the alpha-amino groups of hemoglobin, Effect on functional properties
    • DiDonato, A., Fantl, W. J., Acharya, A. S., and Manning, J. M. (1983) Selective carboxymethylation of the alpha-amino groups of hemoglobin, Effect on functional properties. J. Biol. Chem. 258, 11890-11895.
    • (1983) J. Biol. Chem , vol.258 , pp. 11890-11895
    • DiDonato, A.1    Fantl, W.J.2    Acharya, A.S.3    Manning, J.M.4
  • 14
    • 0021111673 scopus 로고
    • Schiff base adducts of glyceraldehyde with hemoglobin. Differences in the Amadori rearrangement at the alpha-amino groups
    • Acharya, A. S., Sussman, L. G., and Manning, J. M. (1983) Schiff base adducts of glyceraldehyde with hemoglobin. Differences in the Amadori rearrangement at the alpha-amino groups. J. Biol. Chem. 258, 2296-2302.
    • (1983) J. Biol. Chem , vol.258 , pp. 2296-2302
    • Acharya, A.S.1    Sussman, L.G.2    Manning, J.M.3
  • 15
    • 22444438012 scopus 로고    scopus 로고
    • N-terminal acetylation and protonation of individual hemoglobin subunits: Position-dependent effects on tetramer strength and cooperativity
    • Ashiuchi, M., Yagami, T., Willey, R. J., Padovan, J. C., Chait, B. T., Popowicz, A., Manning, L. R., and Manning, J. M. (2005) N-terminal acetylation and protonation of individual hemoglobin subunits: position-dependent effects on tetramer strength and cooperativity. Protein Sci. 14, 1458-1471.
    • (2005) Protein Sci , vol.14 , pp. 1458-1471
    • Ashiuchi, M.1    Yagami, T.2    Willey, R.J.3    Padovan, J.C.4    Chait, B.T.5    Popowicz, A.6    Manning, L.R.7    Manning, J.M.8
  • 16
    • 0024953088 scopus 로고
    • Mechanisms of cooperativity and allosteric regulation in proteins
    • Perutz, M. F. (1989) Mechanisms of cooperativity and allosteric regulation in proteins. Q. Rev. Biophys. 22, 139-237.
    • (1989) Q. Rev. Biophys , vol.22 , pp. 139-237
    • Perutz, M.F.1
  • 17
    • 0028263841 scopus 로고
    • Chloride ion independence of the Bohr effect in a mutant human hemoglobin beta (V1M+H2deleted)
    • Fronticelli, C., Gattoni, M., Lu, A. L., Brinigar, W. S., Bucci, J. L., and Chiancone, E. (1994) Chloride ion independence of the Bohr effect in a mutant human hemoglobin beta (V1M+H2deleted). Biophys. Chem. 51, 53-57.
    • (1994) Biophys. Chem , vol.51 , pp. 53-57
    • Fronticelli, C.1    Gattoni, M.2    Lu, A.L.3    Brinigar, W.S.4    Bucci, J.L.5    Chiancone, E.6
  • 18
    • 0035822702 scopus 로고    scopus 로고
    • Monomer-dimer equilibrium and oxygen binding properties of ferrous Vitreoscilla hemoglobin
    • Giangiacomo, L., D'Avino, R., di Prisco, G., and Chiancone, E. (2001) Monomer-dimer equilibrium and oxygen binding properties of ferrous Vitreoscilla hemoglobin. Biochemistry 40, 3062-3068.
    • (2001) Biochemistry , vol.40 , pp. 3062-3068
    • Giangiacomo, L.1    D'Avino, R.2    di Prisco, G.3    Chiancone, E.4
  • 19
    • 0019514072 scopus 로고
    • Mutual effects of protons, NaCl, and oxygen on the dimer-tetramer assembly of human hemoglobin. The dimer Bohr effect
    • Chu, A. H., and Ackers, G. K. (1981) Mutual effects of protons, NaCl, and oxygen on the dimer-tetramer assembly of human hemoglobin. The dimer Bohr effect. J. Biol. Chem. 256, 1199-1205.
    • (1981) J. Biol. Chem , vol.256 , pp. 1199-1205
    • Chu, A.H.1    Ackers, G.K.2
  • 20
    • 0037124498 scopus 로고    scopus 로고
    • Kinstler, O., Molineux, G., Treuheit, M., Ladd, and D., and Gegg, C. (2002) Mono-N-terminal poly(ethylene glycol)-protein conjugates. Adv. Drug Delivery Rev. 54, 477-485.
    • Kinstler, O., Molineux, G., Treuheit, M., Ladd, and D., and Gegg, C. (2002) Mono-N-terminal poly(ethylene glycol)-protein conjugates. Adv. Drug Delivery Rev. 54, 477-485.
  • 21
    • 0142166336 scopus 로고    scopus 로고
    • Purification and molecular analysis of hemoglobin by high-performance liquid chromatography
    • Manjula, B. N., and Acharya, A. S. (2003) Purification and molecular analysis of hemoglobin by high-performance liquid chromatography. Methods Mol. Med. 82, 31-47.
    • (2003) Methods Mol. Med , vol.82 , pp. 31-47
    • Manjula, B.N.1    Acharya, A.S.2
  • 22
    • 0023024415 scopus 로고
    • Isolation and characterization of a new hemoglobin derivative cross-linked between the α chains (lysine 99R1 -lysine 99α2)
    • Chatterjee, R., Welty, E. V., Walder, R. Y., Pruitt, S. L., Rogers, P. L., Arnone, A., and Walder, J. A. (1986) Isolation and characterization of a new hemoglobin derivative cross-linked between the α chains (lysine 99R1 -lysine 99α2). J. Biol. Chem. 261, 9929-9937.
    • (1986) J. Biol. Chem , vol.261 , pp. 9929-9937
    • Chatterjee, R.1    Welty, E.V.2    Walder, R.Y.3    Pruitt, S.L.4    Rogers, P.L.5    Arnone, A.6    Walder, J.A.7
  • 23
    • 0014679374 scopus 로고
    • Determination of the reactive sulfhydryl groups in heme proteins with 4,4'-dipyridine disulfide
    • Ampulski, R. S., Ayers, V. E., and Morell, S. A. (1969) Determination of the reactive sulfhydryl groups in heme proteins with 4,4'-dipyridine disulfide. Anal. Biochem. 32, 136-169.
    • (1969) Anal. Biochem , vol.32 , pp. 136-169
    • Ampulski, R.S.1    Ayers, V.E.2    Morell, S.A.3
  • 24
    • 0015223254 scopus 로고
    • Dissociation of hemoglobin into subunits. Ligand-linked dissociation at neutral pH
    • Kellett, G. L. (1971) Dissociation of hemoglobin into subunits. Ligand-linked dissociation at neutral pH. J. Mol. Biol. 59, 401-424.
    • (1971) J. Mol. Biol , vol.59 , pp. 401-424
    • Kellett, G.L.1
  • 25
    • 18844427853 scopus 로고    scopus 로고
    • Structural and biophysical characterization of the 40 kDa PEG-interferon-alpha2a and its individual positional isomers
    • Dhalluin, C., Ross, A., Leuthold, L. A., Foser, S., Gsell, B., Muller, F., and Senn, H. (2005) Structural and biophysical characterization of the 40 kDa PEG-interferon-alpha2a and its individual positional isomers. Bioconjugate Chem. 16, 504-517.
    • (2005) Bioconjugate Chem , vol.16 , pp. 504-517
    • Dhalluin, C.1    Ross, A.2    Leuthold, L.A.3    Foser, S.4    Gsell, B.5    Muller, F.6    Senn, H.7
  • 28
    • 0021162143 scopus 로고
    • Solvent regulation of oxygen affinity in hemoglobin. Sensitivity of bovine hemoglobin to chloride ions
    • Fronticelli, C., Bucci, E., and Orth, C. (1984) Solvent regulation of oxygen affinity in hemoglobin. Sensitivity of bovine hemoglobin to chloride ions. J. Biol. Chem. 259, 10841-10844.
    • (1984) J. Biol. Chem , vol.259 , pp. 10841-10844
    • Fronticelli, C.1    Bucci, E.2    Orth, C.3
  • 29
    • 0016833402 scopus 로고
    • Determination of the pK values for the alpha-amino groups of human hemoglobin
    • Garner, M. H., Jr., and Gurd, F. R. (1975) Determination of the pK values for the alpha-amino groups of human hemoglobin. J. Biol. Chem. 250, 4398-4404.
    • (1975) J. Biol. Chem , vol.250 , pp. 4398-4404
    • Garner Jr., M.H.1    Gurd, F.R.2
  • 30
    • 0001209134 scopus 로고    scopus 로고
    • Analytical Ultracentrifugation as a Contemporary Biomolecular Research Tool
    • Cole, J. L., and Hansen, J. C. (1999) Analytical Ultracentrifugation as a Contemporary Biomolecular Research Tool. J. Biomol. Tech. 10, 163-176.
    • (1999) J. Biomol. Tech , vol.10 , pp. 163-176
    • Cole, J.L.1    Hansen, J.C.2
  • 31
    • 0028276739 scopus 로고
    • Stationary and time-resolved circular dichroism of hemoglobins
    • Zentz, C., Pin, S., and Alpert, B. (1994) Stationary and time-resolved circular dichroism of hemoglobins. Methods Enzymol. 232, 247-266.
    • (1994) Methods Enzymol , vol.232 , pp. 247-266
    • Zentz, C.1    Pin, S.2    Alpert, B.3
  • 32
    • 0016258287 scopus 로고
    • Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin
    • Perutz, M. F., Ladner, J. E., Simon, S. R., and Ho, C. (1974) Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin. Biochemistry 13, 2163-2173.
    • (1974) Biochemistry , vol.13 , pp. 2163-2173
    • Perutz, M.F.1    Ladner, J.E.2    Simon, S.R.3    Ho, C.4
  • 33
    • 0015223110 scopus 로고
    • The origin of the heme Cotton effects in myoglobin and hemoglobin
    • Hsu, M. C., and Woody, R. W. (1971) The origin of the heme Cotton effects in myoglobin and hemoglobin. J. Am. Chem. Soc. 93, 3515-3525.
    • (1971) J. Am. Chem. Soc , vol.93 , pp. 3515-3525
    • Hsu, M.C.1    Woody, R.W.2
  • 34
    • 0142228326 scopus 로고    scopus 로고
    • Hemoglobin fluorescence
    • Hirsch, R. E. (2003) Hemoglobin fluorescence. Methods Mol. Med. 82, 133-154.
    • (2003) Methods Mol. Med , vol.82 , pp. 133-154
    • Hirsch, R.E.1
  • 35
    • 33748743556 scopus 로고    scopus 로고
    • Allosteric effectors influence the tetramer stability of both R- and T-states of hemoglobin A
    • Schay, G., Smeller, L., Tsuneshige, A., Yonetani, T., and Fidy, J. (2006) Allosteric effectors influence the tetramer stability of both R- and T-states of hemoglobin A. J. Biol. Chem. 281, 25972-25983.
    • (2006) J. Biol. Chem , vol.281 , pp. 25972-25983
    • Schay, G.1    Smeller, L.2    Tsuneshige, A.3    Yonetani, T.4    Fidy, J.5
  • 36
    • 0017088685 scopus 로고
    • Hemoglobin providence. Functional consequences of two alterations of the 2,3-diphosphoglycerate binding site at position beta 82
    • Bonaventura, J., Bonaventura, C., Sullivan, B., Ferruzzi, G., McCurdy, P. R., Fox, J., and Moo-Penn, M. W. (1976) Hemoglobin providence. Functional consequences of two alterations of the 2,3-diphosphoglycerate binding site at position beta 82. J. Biol. Chem. 251, 7563-7571.
    • (1976) J. Biol. Chem , vol.251 , pp. 7563-7571
    • Bonaventura, J.1    Bonaventura, C.2    Sullivan, B.3    Ferruzzi, G.4    McCurdy, P.R.5    Fox, J.6    Moo-Penn, M.W.7
  • 37
    • 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
    • Dumoulin, A., Manning, L. R., Jenkins, W. T., Winslow, R. M., and Manning, J. M. (1997) 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) J. Biol. Chem , vol.272 , pp. 31326-31332
    • Dumoulin, A.1    Manning, L.R.2    Jenkins, W.T.3    Winslow, R.M.4    Manning, J.M.5
  • 38
  • 39
    • 0019170719 scopus 로고
    • Hemoglobin Rothschild (beta 37(C3)Trp replaced by Arg): A high/low affinity hemoglobin mutant
    • Sharma, V. S., Newton, G. L., Ranney, H. M., Ahmed, F., Harris, J. W., and Danish, E. H. (1980) Hemoglobin Rothschild (beta 37(C3)Trp replaced by Arg): A high/low affinity hemoglobin mutant. J. Mol. Biol. 144, 267-280.
    • (1980) J. Mol. Biol , vol.144 , pp. 267-280
    • Sharma, V.S.1    Newton, G.L.2    Ranney, H.M.3    Ahmed, F.4    Harris, J.W.5    Danish, E.H.6
  • 40
    • 0026200338 scopus 로고
    • Double mixing stopped-flow method for the study of equilibria and kinetics of dimer-tetramer association of hemoglobins: Studies on Hb Carp, Hb A, and Hb Rothschild
    • Berjis, M., and Sharma, V. S. (1991) Double mixing stopped-flow method for the study of equilibria and kinetics of dimer-tetramer association of hemoglobins: studies on Hb Carp, Hb A, and Hb Rothschild. Anal. Biochem. 196, 223-228.
    • (1991) Anal. Biochem , vol.196 , pp. 223-228
    • Berjis, M.1    Sharma, V.S.2
  • 41
    • 0015867359 scopus 로고
    • Kinetic and equilibrium properties of hemoglobin Kansas
    • Gibson, Q. H., Riggs, A., and Imamura, T. (1973) Kinetic and equilibrium properties of hemoglobin Kansas. J. Biol. Chem. 248, 5976-5986.
    • (1973) J. Biol. Chem , vol.248 , pp. 5976-5986
    • Gibson, Q.H.1    Riggs, A.2    Imamura, T.3
  • 42
    • 0014448369 scopus 로고
    • Subunit dissociation of certain abnormal human hemoglobins
    • Bunn, H. F. (1969) Subunit dissociation of certain abnormal human hemoglobins. J. Clin. InVest. 48, 126-138.
    • (1969) J. Clin. InVest , vol.48 , pp. 126-138
    • Bunn, H.F.1
  • 43
    • 0016760252 scopus 로고
    • The crystal structure of human deoxyhaemoglobin at 1.74 A resolution
    • Fermi, G. (1975) The crystal structure of human deoxyhaemoglobin at 1.74 A resolution. J. Mol. Biol. 97, 237-256.
    • (1975) J. Mol. Biol , vol.97 , pp. 237-256
    • Fermi, G.1
  • 44
    • 0022240308 scopus 로고
    • Haemoglobin: The surface buried between the alpha 1 beta 1 and alpha 2 beta 2 dimers in the deoxy and oxy structures
    • Lesk, A. M., Janin, J., Wodak, S., and Chothia, C. (1985) Haemoglobin: the surface buried between the alpha 1 beta 1 and alpha 2 beta 2 dimers in the deoxy and oxy structures. J. Mol. Biol. 183, 267-270.
    • (1985) J. Mol. Biol , vol.183 , pp. 267-270
    • Lesk, A.M.1    Janin, J.2    Wodak, S.3    Chothia, C.4
  • 45
    • 84912295857 scopus 로고
    • X-ray diffraction studies of carbamylated human deoxyhemoglobin
    • Arnone, A., O'Donnell, S., and Schuster, T. (1976) X-ray diffraction studies of carbamylated human deoxyhemoglobin. Fed. Proc. 35, 1604.
    • (1976) Fed. Proc , vol.35 , pp. 1604
    • Arnone, A.1    O'Donnell, S.2    Schuster, T.3


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