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Volumn 23, Issue 6, 2006, Pages 565-572

Influence of allosteric effectors and temperature on oxygen binding properties and the Bohr effect of bovine hemoglobin

Author keywords

Allosteric effector; Bohr effect; Bovine; Hemoglobin; Oxygen transport; Temperature

Indexed keywords

2,3 DIPHOSPHOGLYCERIC ACID; CHLORIDE; HEMOGLOBIN; OXYGEN;

EID: 33748063585     PISSN: 02890003     EISSN: 02890003     Source Type: Journal    
DOI: 10.2108/zsj.23.565     Document Type: Article
Times cited : (7)

References (37)
  • 4
    • 0015210116 scopus 로고
    • Differences in the interaction of 2,3-diphosphoglycerate with certain mammalian hemoglobins
    • Bunn HF (1971) Differences in the interaction of 2,3-diphosphoglycerate with certain mammalian hemoglobins. Science 172: 1049-1050
    • (1971) Science , vol.172 , pp. 1049-1050
    • Bunn, H.F.1
  • 5
    • 0000917199 scopus 로고
    • Regulation of hemoglobin function in mammals
    • Bunn HF (1980) Regulation of hemoglobin function in mammals. Am Zool 20: 199-211
    • (1980) Am Zool , vol.20 , pp. 199-211
    • Bunn, H.F.1
  • 7
    • 0027135394 scopus 로고
    • Comparative study of the oxyhaemoglobin dissociation curve of four mammals: Man, dog, horse and cattle
    • Clerbaux T, Gustin P, Detry B, Cao ML, Frans A (1993) Comparative study of the oxyhaemoglobin dissociation curve of four mammals: man, dog, horse and cattle. Comp Biochem Physiol Comp Physiol 106: 687-694
    • (1993) Comp Biochem Physiol Comp Physiol , vol.106 , pp. 687-694
    • Clerbaux, T.1    Gustin, P.2    Detry, B.3    Cao, M.L.4    Frans, A.5
  • 10
    • 3042702475 scopus 로고    scopus 로고
    • From the arctic to fetal life: Physiological importance and structural basis of an 'additional' chloride-binding site in haemoglobin
    • De Rosa MC, Castagnola M, Bertonati C, Galtieri A, Giardina B (2004) From the arctic to fetal life: physiological importance and structural basis of an 'additional' chloride-binding site in haemoglobin. Biochem J 380: 889-896
    • (2004) Biochem J , vol.380 , pp. 889-896
    • De Rosa, M.C.1    Castagnola, M.2    Bertonati, C.3    Galtieri, A.4    Giardina, B.5
  • 11
    • 0005656280 scopus 로고
    • A modified method for the determination of 2,3-diphosphoglycerate in erythrocytes
    • Ericson A, de Verdier CH (1972) A modified method for the determination of 2,3-diphosphoglycerate in erythrocytes. Scand J Clin Lab Invest 29: 84-90
    • (1972) Scand J Clin Lab Invest , vol.29 , pp. 84-90
    • Ericson, A.1    De Verdier, C.H.2
  • 12
    • 0000400174 scopus 로고
    • Microdetermination of oxyhemoglobin, methemoglobin, and sulfhemoglobin in a single sample of blood
    • Evelyn KA, Malloy HT (1938) Microdetermination of oxyhemoglobin, methemoglobin, and sulfhemoglobin in a single sample of blood. J Biol Chem 126: 655-662
    • (1938) J Biol Chem , vol.126 , pp. 655-662
    • Evelyn, K.A.1    Malloy, H.T.2
  • 14
    • 0021162143 scopus 로고
    • Solvent regulation of oxygen affinity in hemoglobin. Sensitivity of bovine hemoglobin to chloride ions
    • Fronticelli C, Bucci E, 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
  • 15
    • 0029561342 scopus 로고
    • Allosteric modulation by tertiary structure in mammalian hemoglobins. Introduction of the functional characteristics of bovine hemoglobin into human hemoglobin by five amino acid substitutions
    • Fronticelli C, Sanna MT, Perez-Alvarado GC, Karavitis M, Lu AL, Brinigar WS (1995) Allosteric modulation by tertiary structure in mammalian hemoglobins. Introduction of the functional characteristics of bovine hemoglobin into human hemoglobin by five amino acid substitutions. J Biol Chem 270: 30588-30592
    • (1995) J Biol Chem , vol.270 , pp. 30588-30592
    • Fronticelli, C.1    Sanna, M.T.2    Perez-Alvarado, G.C.3    Karavitis, M.4    Lu, A.L.5    Brinigar, W.S.6
  • 17
    • 0025126039 scopus 로고
    • Thermodynamics of oxygen binding to arctic hemoglobins. The case of reindeer
    • Giardina B, Condo SG, Petruzzelli R, Bardgard A, Brix O (1990) Thermodynamics of oxygen binding to arctic hemoglobins. The case of reindeer. Biophys Chem 37: 281-286
    • (1990) Biophys Chem , vol.37 , pp. 281-286
    • Giardina, B.1    Condo, S.G.2    Petruzzelli, R.3    Bardgard, A.4    Brix, O.5
  • 18
    • 0015790339 scopus 로고
    • An enzymatic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriers
    • Hayashi A, Suzuki T, Shin M (1973) An enzymatic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriers. Biochim Biophys Acta 310: 309-316
    • (1973) Biochim Biophys Acta , vol.310 , pp. 309-316
    • Hayashi, A.1    Suzuki, T.2    Shin, M.3
  • 19
    • 0003043542 scopus 로고
    • The possible effects of the aggregation of the molecules of hemoglobin on its oxygen dissociation curve
    • Hill AV (1910) The possible effects of the aggregation of the molecules of hemoglobin on its oxygen dissociation curve. J Physiol 40: 4-7
    • (1910) J Physiol , vol.40 , pp. 4-7
    • Hill, A.V.1
  • 20
    • 0019738497 scopus 로고
    • Measurement of accurate oxygen equilibrium curves by an automatic oxygenation apparatus
    • Imai K (1981) Measurement of accurate oxygen equilibrium curves by an automatic oxygenation apparatus. Meth Enzymol 76: 438-449
    • (1981) Meth Enzymol , vol.76 , pp. 438-449
    • Imai, K.1
  • 21
    • 0016786183 scopus 로고
    • Thermodynamical studies of oxygen equilibrium of hemoglobin. Nonuniform heats and entropy changes for the individual oxygenation steps and enthalpy-entropy compensation
    • Imai K, Yonetani T (1975) Thermodynamical studies of oxygen equilibrium of hemoglobin. Nonuniform heats and entropy changes for the individual oxygenation steps and enthalpy-entropy compensation. J Biol Chem 250: 7093-7098
    • (1975) J Biol Chem , vol.250 , pp. 7093-7098
    • Imai, K.1    Yonetani, T.2
  • 22
    • 0017577243 scopus 로고
    • The hemoglobin-oxygen equilibrium associated with subunit dissociation. 1. An approach with the Hill scheme
    • Imai K, Yonetani T (1977) The hemoglobin-oxygen equilibrium associated with subunit dissociation. 1. 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
  • 23
    • 0035639316 scopus 로고    scopus 로고
    • A new look on the position of the oxygen equilibrium curve of human adult hemoglobin at rest and during exercise with special reference to the effectiveness of the Bohr shift
    • Itoh R, Sasagawa K, Kimura S, Ishigaki K, Imai K, Kobayashi M (2001) A new look on the position of the oxygen equilibrium curve of human adult hemoglobin at rest and during exercise with special reference to the effectiveness of the Bohr shift. Zool Sci 18: 905-908
    • (2001) Zool Sci , vol.18 , pp. 905-908
    • Itoh, R.1    Sasagawa, K.2    Kimura, S.3    Ishigaki, K.4    Imai, K.5    Kobayashi, M.6
  • 25
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plansible model
    • Monod J, Wyman J, Changeux J-P (1965) On the nature of allosteric transitions: a plansible model. J Mol Biol 12: 88-118
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 26
    • 0018860147 scopus 로고
    • Regulation of oxygen affinity of mammalian haemoglobins
    • Perutz MF, Imai K (1980) Regulation of oxygen affinity of mammalian haemoglobins. J Mol Biol 136: 183-191
    • (1980) J Mol Biol , vol.136 , pp. 183-191
    • Perutz, M.F.1    Imai, K.2
  • 27
    • 0027453843 scopus 로고
    • A novel allosteric mechanism in haemoglobin. Structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin
    • Perutz MF, Fermi G, Poyart C, Pagnier J, Kister J (1993) A novel allosteric mechanism in haemoglobin. Structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin. J Mol Biol 233: 536-545
    • (1993) J Mol Biol , vol.233 , pp. 536-545
    • Perutz, M.F.1    Fermi, G.2    Poyart, C.3    Pagnier, J.4    Kister, J.5
  • 30
    • 0020434688 scopus 로고
    • Temperature independence of the alkaline Bohr effect in pig red cells and pig haemoglobin solutions
    • Sinet M, Bohn B, Guesnon P, Poyart C (1982) Temperature independence of the alkaline Bohr effect in pig red cells and pig haemoglobin solutions. Biochim Biophys Acta 708: 105-111
    • (1982) Biochim Biophys Acta , vol.708 , pp. 105-111
    • Sinet, M.1    Bohn, B.2    Guesnon, P.3    Poyart, C.4
  • 31
    • 0018778445 scopus 로고
    • Oxygen binding of fetal and adult bovine hemoglobin in the presence of organic phosphates and uric acid riboside
    • Smith RC, Garbutt GJ, Isaacks RE, Harkness DR (1979) Oxygen binding of fetal and adult bovine hemoglobin in the presence of organic phosphates and uric acid riboside. Hemoglobin 3: 47-55
    • (1979) Hemoglobin , vol.3 , pp. 47-55
    • Smith, R.C.1    Garbutt, G.J.2    Isaacks, R.E.3    Harkness, D.R.4
  • 32
    • 0023204369 scopus 로고
    • Adaptive variation in the mammalian respiratory system in relation to energetic demand: II. Reaching the limits to oxygen flow
    • Taylor CR, Karas RH, Weibel ER, Hoppeler H (1987) Adaptive variation in the mammalian respiratory system in relation to energetic demand: II. Reaching the limits to oxygen flow. Respir Physiol 69: 7-26
    • (1987) Respir Physiol , vol.69 , pp. 7-26
    • Taylor, C.R.1    Karas, R.H.2    Weibel, E.R.3    Hoppeler, H.4
  • 33
    • 0346935206 scopus 로고    scopus 로고
    • A reexamination of the mechanisms underlying the arteriovenous chloride shift
    • Westen EA, Prange HD (2003) A reexamination of the mechanisms underlying the arteriovenous chloride shift. Physiol Biochem Zool 76: 603-614
    • (2003) Physiol Biochem Zool , vol.76 , pp. 603-614
    • Westen, E.A.1    Prange, H.D.2
  • 34
    • 0022616633 scopus 로고
    • Modest effect of temperature on the porcine oxygen dissociation curve
    • Willford DC, Hill EP (1986) Modest effect of temperature on the porcine oxygen dissociation curve. Respir Physiol 64: 113-123
    • (1986) Respir Physiol , vol.64 , pp. 113-123
    • Willford, D.C.1    Hill, E.P.2
  • 35
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • Wyman J (1964) Linked functions and reciprocal effects in hemoglobin: a second look. Advan Protein Chem 19: 223-286
    • (1964) Advan Protein Chem , vol.19 , pp. 223-286
    • Wyman, J.1
  • 36
    • 0346973882 scopus 로고    scopus 로고
    • Significance of affinity and cooperativity in oxygen binding to hemoglobin of horse fetal and maternal blood
    • Zhang Y, Kobayashi K, Sasagawa K, Imai K, Kobayashi M (2003a) Significance of affinity and cooperativity in oxygen binding to hemoglobin of horse fetal and maternal blood. Zool Sci 20: 1087-1093
    • (2003) Zool Sci , vol.20 , pp. 1087-1093
    • Zhang, Y.1    Kobayashi, K.2    Sasagawa, K.3    Imai, K.4    Kobayashi, M.5
  • 37
    • 0038105021 scopus 로고    scopus 로고
    • The cooperativity of human fetal and adult hemoglobins is optimized: A consideration based on the effectiveness of the Bohr shift
    • Zhang Y, Miki M, Sasagawa K, Kobayashi M, Imai K, Kobayashi M (2003b) The cooperativity of human fetal and adult hemoglobins is optimized: a consideration based on the effectiveness of the Bohr shift. Zool Sci 20: 23-29
    • (2003) Zool Sci , vol.20 , pp. 23-29
    • Zhang, Y.1    Miki, M.2    Sasagawa, K.3    Kobayashi, M.4    Imai, K.5    Kobayashi, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.