메뉴 건너뛰기




Volumn 7, Issue 3, 1998, Pages 673-680

Tetramer-dimer equilibrium of oxyhemoglobin mutants determined from auto-oxidation rates

Author keywords

Auto oxidation; Hemoglobin; Oxyhemoglobin; Recombinant hemoglobin; Tetramer dimer equilibrium

Indexed keywords

DIMER; HEMOGLOBIN; OXYHEMOGLOBIN; PHYTIC ACID; TETRAMER;

EID: 0031936592     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070316     Document Type: Article
Times cited : (55)

References (65)
  • 4
    • 0017186962 scopus 로고
    • Tetramer-dimer dissociation in hemoglobin and the Bohr effect
    • Atha DH, Riggs A. 1976. Tetramer-dimer dissociation in hemoglobin and the Bohr effect. J Biol Chem 251:5537-5543.
    • (1976) J Biol Chem , vol.251 , pp. 5537-5543
    • Atha, D.H.1    Riggs, A.2
  • 5
    • 0029930628 scopus 로고    scopus 로고
    • Production of super-oxide from hemoglobin-bound oxygen under hypoxic conditions
    • Balagopalakrishna C, Manoharan PT, Abugo OO, Rifkind JM. 1996. Production of super-oxide from hemoglobin-bound oxygen under hypoxic conditions. Biochemistry 35:6393-6398.
    • (1996) Biochemistry , vol.35 , pp. 6393-6398
    • Balagopalakrishna, C.1    Manoharan, P.T.2    Abugo, O.O.3    Rifkind, J.M.4
  • 6
    • 84915592633 scopus 로고
    • Modulation of the ligand reactivity of heme-proteins
    • Gold Sands, Bulgaria
    • Banerjee R, Stetzkowski F, Lhoste JM. 1978. Modulation of the ligand reactivity of heme-proteins. IUPAC Symposium (Gold Sands, Bulgaria) part 2:72-89.
    • (1978) IUPAC Symposium , Issue.2 PART , pp. 72-89
    • Banerjee, R.1    Stetzkowski, F.2    Lhoste, J.M.3
  • 7
    • 0026768252 scopus 로고
    • Allosteric properties of haemoglobin β41 (C7) Phe → Tyr: A stable, low oxygen-affinity variant synthesized in Escherichia coli
    • Baudin V, Pagnier J, Lacaze N, Bihoreau M-T, Kister J, Marden M, Kiger L, Poyart C. 1992. Allosteric properties of haemoglobin β41 (C7) Phe → Tyr: A stable, low oxygen-affinity variant synthesized in Escherichia coli. Biochim Biophys Acta 1159:223-226.
    • (1992) Biochim Biophys Acta , vol.1159 , pp. 223-226
    • Baudin, V.1    Pagnier, J.2    Lacaze, N.3    Bihoreau, M.-T.4    Kister, J.5    Marden, M.6    Kiger, L.7    Poyart, C.8
  • 8
    • 0023832476 scopus 로고
    • Investigation of the tetramer-dimer equilibrium in haemoglobin solutions by high-performance size-exclusion chromatography on a diol column
    • Baudin-Chich V, Marden M, Wajcman H. 1988. Investigation of the tetramer-dimer equilibrium in haemoglobin solutions by high-performance size-exclusion chromatography on a diol column. J Chromatogr 437:193-201.
    • (1988) J Chromatogr , vol.437 , pp. 193-201
    • Baudin-Chich, V.1    Marden, M.2    Wajcman, H.3
  • 9
    • 0025122955 scopus 로고
    • The stability of the heme-globin linkage in some normal, mutant, and chemically modified hemoglobins
    • Benesch RE, Kwong S. 1990. The stability of the heme-globin linkage in some normal, mutant, and chemically modified hemoglobins. J Biol Chem 265:14881-14885.
    • (1990) J Biol Chem , vol.265 , pp. 14881-14885
    • Benesch, R.E.1    Kwong, S.2
  • 10
    • 0029016290 scopus 로고
    • Coupled reactions in hemoglobin. Heme-globin and dimer-dimer association
    • Benesch RE, Kwong S. 1995. Coupled reactions in hemoglobin. Heme-globin and dimer-dimer association. J Biol Chem 270:13785-13786.
    • (1995) J Biol Chem , vol.270 , pp. 13785-13786
    • Benesch, R.E.1    Kwong, S.2
  • 12
    • 0014408665 scopus 로고
    • Hemoglobin Kansas, a human hemoglobin with a neutral amino acid substitution and abnormal oxygen equilibrium
    • Bonaventura J, Riggs A. 1968. Hemoglobin Kansas, a human hemoglobin with a neutral amino acid substitution and abnormal oxygen equilibrium. J Biol Chem 243:980-991.
    • (1968) J Biol Chem , vol.243 , pp. 980-991
    • Bonaventura, J.1    Riggs, A.2
  • 15
    • 0014448369 scopus 로고
    • Subunit dissociation of certain abnormal human hemoglobins
    • Bunn HF. 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
  • 17
    • 0014408353 scopus 로고
    • Exchange of heme among hemoglobins and between hemoglobin and albumin
    • Bunn HF, Jandl JH. 1968. Exchange of heme among hemoglobins and between hemoglobin and albumin. J Biol Chem 243:465-475.
    • (1968) J Biol Chem , vol.243 , pp. 465-475
    • Bunn, H.F.1    Jandl, J.H.2
  • 19
    • 0014429239 scopus 로고
    • Dissociation of hemoglobin into subunits. II. Human oxyhemoglobin: Gel filtration studies
    • Chiancone E, Gilbert LM, Kellett GL. 1968. Dissociation of hemoglobin into subunits. II. Human oxyhemoglobin: Gel filtration studies. J Biol Chem 243:1212-1219.
    • (1968) J Biol Chem , vol.243 , pp. 1212-1219
    • Chiancone, E.1    Gilbert, L.M.2    Kellett, G.L.3
  • 20
    • 0019514072 scopus 로고
    • Mutual effects of protons, NaCl, and oxygen on the dimer-tetramer assembly of human hemoglobin. The dimer Bohr effect
    • Chu AH, Ackers GK. 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
  • 21
    • 0000564980 scopus 로고
    • The electron-transfer mechanism of autoxidation for hemoglobin, myoglobin, and their iron (II) cyclidene models
    • Dickerson LD, Sauer-Masarwa A, Herron N, Fendrick CM, Busch DH. 1993. The electron-transfer mechanism of autoxidation for hemoglobin, myoglobin, and their iron (II) cyclidene models. J Am Chem Soc 115:3623-3626.
    • (1993) J Am Chem Soc , vol.115 , pp. 3623-3626
    • Dickerson, L.D.1    Sauer-Masarwa, A.2    Herron, N.3    Fendrick, C.M.4    Busch, D.H.5
  • 22
    • 0026496538 scopus 로고
    • Cooperative oxygen binding, subunit assembly, and sulfhydryl reaction kinetics of the eight cyanomet intermediate ligation states of human hemoglobin
    • Doyle ML, Ackers GK. 1992. Cooperative oxygen binding, subunit assembly, and sulfhydryl reaction kinetics of the eight cyanomet intermediate ligation states of human hemoglobin. Biochemistry 31:11182-11195.
    • (1992) Biochemistry , vol.31 , pp. 11182-11195
    • Doyle, M.L.1    Ackers, G.K.2
  • 24
    • 0000448117 scopus 로고
    • The oxidation of myoglobin to metmyoglobin by oxygen. The relation between the first order rate constant and the partial pressure of oxygen
    • George P, Stratmann CJ. 1952. The oxidation of myoglobin to metmyoglobin by oxygen. The relation between the first order rate constant and the partial pressure of oxygen. Biochem J 51:418-425.
    • (1952) Biochem J , vol.51 , pp. 418-425
    • George, P.1    Stratmann, C.J.2
  • 25
    • 0014966591 scopus 로고
    • Differential sedimentation study on the dissociation and conformational change in hemoglobin
    • Goers JW, Schumaker VN. 1970. Differential sedimentation study on the dissociation and conformational change in hemoglobin. J Mol Biol 54:125-129.
    • (1970) J Mol Biol , vol.54 , pp. 125-129
    • Goers, J.W.1    Schumaker, V.N.2
  • 26
    • 0016137782 scopus 로고
    • The effect of 2,3-diphosphoglycerate on the tetramer-dimer equilibrium of liganded hemoglobin
    • Gray RD. 1974. The effect of 2,3-diphosphoglycerate on the tetramer-dimer equilibrium of liganded hemoglobin. J Biol Chem 249:2879-2885.
    • (1974) J Biol Chem , vol.249 , pp. 2879-2885
    • Gray, R.D.1
  • 27
    • 0019320859 scopus 로고
    • +, inositol hexaphosphate, and Zn(II) on the tetramer-dimer equilibrium of liganded hemoglobin
    • +, inositol hexaphosphate, and Zn(II) on the tetramer-dimer equilibrium of liganded hemoglobin. J Biol Chem 255:1812-1818.
    • (1980) J Biol Chem , vol.255 , pp. 1812-1818
    • Gray, R.D.1
  • 28
    • 0023665351 scopus 로고
    • The effect of 2,3-diphosphoglycerate on the tetramer-dimer equilibrium of carbon monoxide hemoglobin in dilute solution. Correlation between sedimentation and kinetic behavior
    • Gray RD, Dean WL. 1987. The effect of 2,3-diphosphoglycerate on the tetramer-dimer equilibrium of carbon monoxide hemoglobin in dilute solution. Correlation between sedimentation and kinetic behavior. J Biol Chem 262:15890-15893.
    • (1987) J Biol Chem , vol.262 , pp. 15890-15893
    • Gray, R.D.1    Dean, W.L.2
  • 32
    • 0017577243 scopus 로고
    • The hemoglobin-oxygen equilibrium associated with subunit dissociation. An approach with the Hill scheme
    • Imai K, Yonetani T. 1977. The hemoglobin-oxygen equilibrium associated with subunit dissociation. An approach with the Hill scheme. Biochim Biophys Acta 490:164-170.
    • (1977) Biochim Biophys Acta , vol.490 , pp. 164-170
    • Imai, K.1    Yonetani, T.2
  • 33
    • 0017352615 scopus 로고
    • Thermodynamic studies on subunit assembly in human hemoglobin. Temperature dependence of the dimer-tetramer association constants for oxygenated and unliganded hemoglobins
    • Ip SH, Ackers GK. 1977. Thermodynamic studies on subunit assembly in human hemoglobin. Temperature dependence of the dimer-tetramer association constants for oxygenated and unliganded hemoglobins. J Biol Chem 252:82-87.
    • (1977) J Biol Chem , vol.252 , pp. 82-87
    • Ip, S.H.1    Ackers, G.K.2
  • 34
    • 0023900648 scopus 로고
    • Photolysis method for determination of the tetramer-dimer dissociation constant of deoxyhemoglobin
    • Khaleque MA, Sawicki CA. 1988. Photolysis method for determination of the tetramer-dimer dissociation constant of deoxyhemoglobin. J Biochem Biophys Methods 16:41-48.
    • (1988) J Biochem Biophys Methods , vol.16 , pp. 41-48
    • Khaleque, M.A.1    Sawicki, C.A.2
  • 35
    • 2642615723 scopus 로고
    • Haemoglobin Toulouse β66(E 10) Lys → Glu: Structure and consequences in molecular pathology
    • Labie D, Rosa J, Belkhodja O. 1971. Haemoglobin Toulouse β66(E 10) Lys → Glu: Structure and consequences in molecular pathology. Br J Haematol 20:672.
    • (1971) Br J Haematol , vol.20 , pp. 672
    • Labie, D.1    Rosa, J.2    Belkhodja, O.3
  • 36
    • 0028264418 scopus 로고
    • Measuring relative rates of hemoglobin oxidation and denaturation
    • MacDonald VW. 1994. Measuring relative rates of hemoglobin oxidation and denaturation. Methods Enzymol 231:480-490.
    • (1994) Methods Enzymol , vol.231 , pp. 480-490
    • MacDonald, V.W.1
  • 37
    • 51249177497 scopus 로고
    • Mechanism of autoxidation of oxyhaemoglobin
    • Mal A, Chatterjee IB. 1991. Mechanism of autoxidation of oxyhaemoglobin. J Biosci 16:55-70.
    • (1991) J Biosci , vol.16 , pp. 55-70
    • Mal, A.1    Chatterjee, I.B.2
  • 39
    • 0025996464 scopus 로고
    • Coupling of ferric iron spin and allosteric equilibrium in hemoglobin
    • Marden MC, Kiger L, Kister J, Bohn B, Poyart C. 1991. Coupling of ferric iron spin and allosteric equilibrium in hemoglobin. Biophys J 60:770-776.
    • (1991) Biophys J , vol.60 , pp. 770-776
    • Marden, M.C.1    Kiger, L.2    Kister, J.3    Bohn, B.4    Poyart, C.5
  • 40
    • 0029449471 scopus 로고
    • Oxygen delivery and autoxidation of hemoglobin
    • Marden MC, Griffon N, Poyart C. 1995. Oxygen delivery and autoxidation of hemoglobin. Trans Clin Biol 6:473-480.
    • (1995) Trans Clin Biol , vol.6 , pp. 473-480
    • Marden, M.C.1    Griffon, N.2    Poyart, C.3
  • 41
    • 49149143246 scopus 로고
    • Analysis of protein association by partitioning in aqueous two-phase polymer systems: Applications to the tetramer-dimer dissociation of hemoglobin
    • Middaugh CR, Lawson EQ. 1980. Analysis of protein association by partitioning in aqueous two-phase polymer systems: Applications to the tetramer-dimer dissociation of hemoglobin. Anal Biochem 105:364-368.
    • (1980) Anal Biochem , vol.105 , pp. 364-368
    • Middaugh, C.R.1    Lawson, E.Q.2
  • 42
    • 0018778777 scopus 로고
    • Thermodynamic studies on the oxygenation and subunit association of human hemoglobin. Temperature dependence of the linkage between dimer-tetramer association and oxygenation state
    • Mills FC, Ackers GK. 1979. Thermodynamic studies on the oxygenation and subunit association of human hemoglobin. Temperature dependence of the linkage between dimer-tetramer association and oxygenation state. J Biol Chem 254:2881-2887.
    • (1979) J Biol Chem , vol.254 , pp. 2881-2887
    • Mills, F.C.1    Ackers, G.K.2
  • 43
    • 0017138398 scopus 로고
    • Oxygenation-linked subunit interactions in human hemoglobin experimental studies on the concentration dependence of oxygenation curves
    • Mills FC, Johnson ML, Ackers GK. 1976. Oxygenation-linked subunit interactions in human hemoglobin experimental studies on the concentration dependence of oxygenation curves. Biochemistry 15:5350-5361.
    • (1976) Biochemistry , vol.15 , pp. 5350-5361
    • Mills, F.C.1    Johnson, M.L.2    Ackers, G.K.3
  • 44
    • 0021153567 scopus 로고
    • Generation of β-globin by sequence specific proteolysis of a hybrid protein produced in Escherichia coli
    • Nagai K, Thogersen HC. 1984. Generation of β-globin by sequence specific proteolysis of a hybrid protein produced in Escherichia coli. Nature 309:810-812.
    • (1984) Nature , vol.309 , pp. 810-812
    • Nagai, K.1    Thogersen, H.C.2
  • 45
    • 0015216974 scopus 로고
    • The binding of haemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin
    • Nagel RL, Gibson QH. 1971. The binding of haemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin. J Biol Chem 246:69-73.
    • (1971) J Biol Chem , vol.246 , pp. 69-73
    • Nagel, R.L.1    Gibson, Q.H.2
  • 47
    • 0025670588 scopus 로고
    • Hemoglobin Saint Mandé [β102 (G4) Asn → Tyr]. Functional studies and structural modeling reveal an altered T state
    • Poyart C, Schaad O, Kister J, Galacteros F, Edelstein SJ, Blouquit Y, Arous N. 1990. Hemoglobin Saint Mandé [β102 (G4) Asn → Tyr]. Functional studies and structural modeling reveal an altered T state. Eur J Biochem 194:343-348.
    • (1990) Eur J Biochem , vol.194 , pp. 343-348
    • Poyart, C.1    Schaad, O.2    Kister, J.3    Galacteros, F.4    Edelstein, S.J.5    Blouquit, Y.6    Arous, N.7
  • 48
    • 0014219346 scopus 로고
    • On the mechanism of the dissociation of haemoglobin
    • Rosemeyer MA, Huens ER. 1967. On the mechanism of the dissociation of haemoglobin. J Mol Biol 25:253-273.
    • (1967) J Mol Biol , vol.25 , pp. 253-273
    • Rosemeyer, M.A.1    Huens, E.R.2
  • 49
    • 0019811330 scopus 로고
    • Autoxidation of oxymyoglobin. A nucleophilic displacement mechanism
    • Satoh Y, Shikama K. 1981. Autoxidation of oxymyoglobin. A nucleophilic displacement mechanism. J Biol Chem 256:10272-10275.
    • (1981) J Biol Chem , vol.256 , pp. 10272-10275
    • Satoh, Y.1    Shikama, K.2
  • 50
    • 0019453294 scopus 로고
    • Tetramer-dimer dissociation of carboxyhemoglobin in the absence of dithionite
    • Sawicki CA, Gibson QH. 1981. Tetramer-dimer dissociation of carboxyhemoglobin in the absence of dithionite. Biophys J 35:265-270.
    • (1981) Biophys J , vol.35 , pp. 265-270
    • Sawicki, C.A.1    Gibson, Q.H.2
  • 51
    • 0023719501 scopus 로고
    • Osmotic pressure measurements of the ligand-linked dissociation equilibrium of human oxyhemoglobin
    • Schönert H, Stoll B. 1988. Osmotic pressure measurements of the ligand-linked dissociation equilibrium of human oxyhemoglobin. Eur J Biochem 176:319-325.
    • (1988) Eur J Biochem , vol.176 , pp. 319-325
    • Schönert, H.1    Stoll, B.2
  • 53
    • 0023582036 scopus 로고
    • Hemoglobin Chico [β66(E10) Lys → Thr]: A new variant with decreased oxygen affinity
    • Shih DTB, Jones RT, Shih, MFC. 1987. Hemoglobin Chico [β66(E10) Lys → Thr]: A new variant with decreased oxygen affinity. Hemoglobin 11:453-464.
    • (1987) Hemoglobin , vol.11 , pp. 453-464
    • Shih, D.T.B.1    Jones, R.T.2    Shih, M.F.C.3
  • 55
    • 0027483635 scopus 로고
    • Autooxidation of hemoglobin: Kinetic analysis of the pH-profile
    • Sugawara Y, Sakoda M, Shibata N, Sakamoto H. 1993. Autooxidation of hemoglobin: Kinetic analysis of the pH-profile. Jpn J Physiol 43:21-34.
    • (1993) Jpn J Physiol , vol.43 , pp. 21-34
    • Sugawara, Y.1    Sakoda, M.2    Shibata, N.3    Sakamoto, H.4
  • 56
    • 0015524222 scopus 로고
    • Observation of the dissociation of unliganded hemoglobin
    • Thomas JO, Edelstein SJ. 1972. Observation of the dissociation of unliganded hemoglobin. J Biol Chem 247:7870-7874.
    • (1972) J Biol Chem , vol.247 , pp. 7870-7874
    • Thomas, J.O.1    Edelstein, S.J.2
  • 57
    • 0018175940 scopus 로고
    • Studies on the subunit dissociation of deoxyhemoglobin using hemoglobin-haptoglobin interactions
    • Tsapis A, Thillet J, Rosa J. 1978. Studies on the subunit dissociation of deoxyhemoglobin using hemoglobin-haptoglobin interactions. Biochem Biophys Res Commun 85:511-516.
    • (1978) Biochem Biophys Res Commun , vol.85 , pp. 511-516
    • Tsapis, A.1    Thillet, J.2    Rosa, J.3
  • 58
    • 0031552067 scopus 로고    scopus 로고
    • Biphasic nature in the autoxidation reaction of human oxyhemoglobin
    • Tsuruga M, Shikama K. 1997. Biphasic nature in the autoxidation reaction of human oxyhemoglobin. Biochem Biophys Acta 1337:96-104.
    • (1997) Biochem Biophys Acta , vol.1337 , pp. 96-104
    • Tsuruga, M.1    Shikama, K.2
  • 62
    • 0016613465 scopus 로고
    • The molecular dissociation of ferrihemoglobin derivatives
    • White SL. 1975. The molecular dissociation of ferrihemoglobin derivatives. J Biol Chem 250:1263-1268.
    • (1975) J Biol Chem , vol.250 , pp. 1263-1268
    • White, S.L.1
  • 63
    • 0017303540 scopus 로고
    • Saturation of the carboxyhemoglobin telramer-dimer equilibrium by inositol hexaphosphate
    • White SL. 1976. Saturation of the carboxyhemoglobin telramer-dimer equilibrium by inositol hexaphosphate. J Biol Chem 251:4763-4769.
    • (1976) J Biol Chem , vol.251 , pp. 4763-4769
    • White, S.L.1
  • 64
    • 0028948671 scopus 로고
    • A recombinant human hemoglobin with asparagine-102(β) substituted by alanine has a limiting low oxygen affinity, reduced marginally by chloride
    • Yanase H, Manning LR, Vandegriff K, Winslow RM, Manning JM. 1995. A recombinant human hemoglobin with asparagine-102(β) substituted by alanine has a limiting low oxygen affinity, reduced marginally by chloride. Protein Sci 4:21-28.
    • (1995) Protein Sci , vol.4 , pp. 21-28
    • Yanase, H.1    Manning, L.R.2    Vandegriff, K.3    Winslow, R.M.4    Manning, J.M.5
  • 65
    • 0026354021 scopus 로고
    • Autoxidation of hemoglobin enhanced by dissociation into dimers
    • Zhang L, Levy A, Rifkind JM. 1991. Autoxidation of hemoglobin enhanced by dissociation into dimers. J Biol Chem 266:24698-24701.
    • (1991) J Biol Chem , vol.266 , pp. 24698-24701
    • Zhang, L.1    Levy, A.2    Rifkind, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.