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Volumn 144, Issue 2-3 SPEC. ISS., 2004, Pages 141-159

Functional adaptation and its molecular basis in vertebrate hemoglobins, neuroglobins and cytoglobins

Author keywords

Adaptation; Allosteric interactions; Cytoglobin; Functional adaptation; Hemoglobin; Neuroglobin; Oxygen binding; Vertebrate globins

Indexed keywords

GLOBIN; HEMOGLOBIN; MEMBRANE PROTEIN; NITRIC OXIDE; OXIDE; WATER;

EID: 7944231804     PISSN: 15699048     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.resp.2004.04.018     Document Type: Conference Paper
Times cited : (122)

References (148)
  • 1
    • 0015997903 scopus 로고
    • Mechanism of action of hemoglobin
    • A. Arnone Mechanism of action of hemoglobin Ann. Rev. Med. 25 1974 123 130
    • (1974) Ann. Rev. Med. , vol.25 , pp. 123-130
    • Arnone, A.1
  • 4
    • 0027523448 scopus 로고
    • Hydration and allosteric transitions in hemoglobin
    • A. Bellelli, A. Brancaccio, and M. Brunori Hydration and allosteric transitions in hemoglobin J. Biol. Chem. 268 1993 4742 4744
    • (1993) J. Biol. Chem. , vol.268 , pp. 4742-4744
    • Bellelli, A.1    Brancaccio, A.2    Brunori, M.3
  • 5
    • 0014985250 scopus 로고
    • Studies on the functional properties of fish hemoglobins. II. the oxygen equilibrium of the isolated hemoglobin components from trout blood
    • I. Binotti, S. Giovenco, B. Giardina, E. Antonini, M. Brunori, and J. Wyman Studies on the functional properties of fish hemoglobins. II. The oxygen equilibrium of the isolated hemoglobin components from trout blood Arch. Biochem. Biophys. 142 1971 274 280
    • (1971) Arch. Biochem. Biophys. , vol.142 , pp. 274-280
    • Binotti, I.1    Giovenco, S.2    Giardina, B.3    Antonini, E.4    Brunori, M.5    Wyman, J.6
  • 6
    • 84935023004 scopus 로고
    • Über einen in biologischer Beziehung wichtigen Einfluss, den die Kohlensaurespannung des Blutes auf dessen Sauerstoffbindung ubt
    • C. Bohr, K. Hasselbalch, and A. Krogh Über einen in biologischer Beziehung wichtigen Einfluss, den die Kohlensaurespannung des Blutes auf dessen Sauerstoffbindung ubt Skand. Arch. Physiol. 16 1904 402 412
    • (1904) Skand. Arch. Physiol. , vol.16 , pp. 402-412
    • Bohr, C.1    Hasselbalch, K.2    Krogh, A.3
  • 8
    • 0037177797 scopus 로고    scopus 로고
    • Heme redox properties of S-nitrosated hemoglobin A(0) and hemoglobin S - Implications for interactions of nitric oxide with normal and sickle red blood cells
    • C. Bonaventura, C.H. Taboy, P.S. Low, R.D. Stevens, C. Lafon, and A.L. Crumbliss Heme redox properties of S-nitrosated hemoglobin A(0) and hemoglobin S - implications for interactions of nitric oxide with normal and sickle red blood cells J. Biol. Chem. 277 2002 14557 14563
    • (2002) J. Biol. Chem. , vol.277 , pp. 14557-14563
    • Bonaventura, C.1    Taboy, C.H.2    Low, P.S.3    Stevens, R.D.4    Lafon, C.5    Crumbliss, A.L.6
  • 9
    • 33746010547 scopus 로고    scopus 로고
    • Nitric oxide invertebrates and hemoglobin
    • J. Bonaventura, and V.P. Lance Nitric oxide invertebrates and hemoglobin Am. Zool. 41 2001 346 359
    • (2001) Am. Zool. , vol.41 , pp. 346-359
    • Bonaventura, J.1    Lance, V.P.2
  • 10
    • 7944224443 scopus 로고    scopus 로고
    • New insights into the proton-dependent oxygen affinity of Root effect hemoglobins
    • in press.
    • Bonaventura, C., Crumbliss, A.L., Weber, R.E., New insights into the proton-dependent oxygen affinity of Root effect hemoglobins. Acta Physiol. Scand., in press.
    • Acta Physiol. Scand.
    • Bonaventura, C.1    Crumbliss, A.L.2    Weber, R.E.3
  • 11
    • 0023161926 scopus 로고
    • Control of cell volume and ion transport by beta-adrenergic catecholamines in erythrocytes of rainbow trout Salmo gairdneri
    • F. Borgese, F. Garcia Romeu, and R. Motais Control of cell volume and ion transport by beta-adrenergic catecholamines in erythrocytes of rainbow trout Salmo gairdneri J. Physiol., London 382 1987 123 144
    • (1987) J. Physiol., London , vol.382 , pp. 123-144
    • Borgese, F.1    Garcia Romeu, F.2    Motais, R.3
  • 13
    • 0009892750 scopus 로고
    • Effects of open- and closed-system temperature changes on blood oxygen dissociation curves of skipjack tuna, Katsuwonus pelamis, and yellowfin tuna, Thunnus albacares
    • R.W. Brill, and P.G. Bushnell Effects of open- and closed-system temperature changes on blood oxygen dissociation curves of skipjack tuna, Katsuwonus pelamis, and yellowfin tuna, Thunnus albacares Can. J. Zool. 69 1991 1814 1821
    • (1991) Can. J. Zool. , vol.69 , pp. 1814-1821
    • Brill, R.W.1    Bushnell, P.G.2
  • 14
    • 0015210116 scopus 로고
    • Differences in the interaction of 2 3-diphosphoglycerate with certain mammalian hemoglobins
    • H.F. Bunn Differences in the interaction of 2 3-diphosphoglycerate with certain mammalian hemoglobins Science 172 1971 1049 1050
    • (1971) Science , vol.172 , pp. 1049-1050
    • Bunn, H.F.1
  • 15
  • 16
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: A novel globin type ubiquitously expressed in vertebrate tissues
    • T. Burmester, B. Ebner, B. Weich, and T. Hankeln Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues Mol. Biol. E 19 2002 416 421
    • (2002) Mol. Biol. e , vol.19 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 17
    • 0026535070 scopus 로고
    • Protein solvation in allosteric regulation: A water effect on hemoglobin
    • M.F. Colombo, D.C. Rau, and V.A. Parsegian Protein solvation in allosteric regulation: a water effect on hemoglobin Science 256 1992 655 659
    • (1992) Science , vol.256 , pp. 655-659
    • Colombo, M.F.1    Rau, D.C.2    Parsegian, V.A.3
  • 18
    • 0029867430 scopus 로고    scopus 로고
    • The water effect on allosteric regulation of hemoglobin probed in water glucose and water glycine solutions
    • M.F. Colombo, and G.O. Bonilla-Rodriguez The water effect on allosteric regulation of hemoglobin probed in water glucose and water glycine solutions J. Biol. Chem. 271 1996 4895 4899
    • (1996) J. Biol. Chem. , vol.271 , pp. 4895-4899
    • Colombo, M.F.1    Bonilla-Rodriguez, G.O.2
  • 22
    • 0023159916 scopus 로고
    • Hagfish (Eptatretus stouti) erythrocytes show minimal chloride transport activity
    • J.C. Ellory, M.W. Wolowyk, and J.D. Young Hagfish (Eptatretus stouti) erythrocytes show minimal chloride transport activity J. Exp. Biol. 129 1987 377 383
    • (1987) J. Exp. Biol. , vol.129 , pp. 377-383
    • Ellory, J.C.1    Wolowyk, M.W.2    Young, J.D.3
  • 23
    • 0029042065 scopus 로고
    • The hemoglobin system of the hagfish Myxine glutinosa: Aggregation state and functional properties
    • A. Fago, and R.E. Weber The hemoglobin system of the hagfish Myxine glutinosa: aggregation state and functional properties Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. 1249 1995 109 115
    • (1995) Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. , vol.1249 , pp. 109-115
    • Fago, A.1    Weber, R.E.2
  • 24
    • 0029163616 scopus 로고
    • The cathodic hemoglobin of Anguilla anguilla amino acid sequence and oxygen equilibria of a reverse Bohr effect hemoglobin with high oxygen affinity and high phosphate sensitivity
    • A. Fago, V. Carratore, G. Di Prisco, R.J. Feuerlein, L. Sottrup-Jensen, and R.E. Weber The cathodic hemoglobin of Anguilla anguilla amino acid sequence and oxygen equilibria of a reverse Bohr effect hemoglobin with high oxygen affinity and high phosphate sensitivity J. Biol. Chem. 270 1995 18897 18902
    • (1995) J. Biol. Chem. , vol.270 , pp. 18897-18902
    • Fago, A.1    Carratore, V.2    Di Prisco, G.3    Feuerlein, R.J.4    Sottrup-Jensen, L.5    Weber, R.E.6
  • 25
    • 0030905324 scopus 로고    scopus 로고
    • The anodic hemoglobin of Anguilla anguilla. Molecular basis for allosteric effects in a Root-effect hemoglobin
    • A. Fago, E. Bendixen, H. Malte, and R.E. Weber The anodic hemoglobin of Anguilla anguilla. Molecular basis for allosteric effects in a Root-effect hemoglobin J. Biol. Chem. 272 1997 15628 15635
    • (1997) J. Biol. Chem. , vol.272 , pp. 15628-15635
    • Fago, A.1    Bendixen, E.2    Malte, H.3    Weber, R.E.4
  • 26
    • 0006571672 scopus 로고    scopus 로고
    • J.M. Jørgensen J.P. Lomholt R.E. Weber H. Malte Chapman & Hall London
    • A. Fago, and R.E. Weber J.M. Jørgensen J.P. Lomholt R.E. Weber H. Malte Hagfish Haemoglobins 1998 Chapman & Hall London pp. 321-333
    • (1998) Hagfish Haemoglobins
    • Fago, A.1    Weber, R.E.2
  • 27
    • 0033036755 scopus 로고    scopus 로고
    • Bicarbonate binding to hemoglobin links oxygen and carbon dioxide transport in hagfish
    • A. Fago, H. Malte, and N. Dohn Bicarbonate binding to hemoglobin links oxygen and carbon dioxide transport in hagfish Respir. Physiol. 115 1999 309 315
    • (1999) Respir. Physiol. , vol.115 , pp. 309-315
    • Fago, A.1    Malte, H.2    Dohn, N.3
  • 29
    • 0142123122 scopus 로고    scopus 로고
    • The case of the missing NO-hemoglobin: Spectral changes suggestive of heme redox reactions reflect changes in NO-heme geometry
    • A. Fago, A.L. Crumbliss, J. Peterson, L.L. Pearce, and C. Bonaventura The case of the missing NO-hemoglobin: spectral changes suggestive of heme redox reactions reflect changes in NO-heme geometry Proc. Natl. Acad. Sci. U.S.A. 100 2003 12087 12092
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12087-12092
    • Fago, A.1    Crumbliss, A.L.2    Peterson, J.3    Pearce, L.L.4    Bonaventura, C.5
  • 31
    • 0035059884 scopus 로고    scopus 로고
    • Oxygen binding by single red blood cells from the red-eared turtle Trachemys scripta
    • S. Frische, S. Bruno, A. Fago, R.E. Weber, and A. Mozzarelli Oxygen binding by single red blood cells from the red-eared turtle Trachemys scripta J. Appl. Physiol. 90 2001 1679 1684
    • (2001) J. Appl. Physiol. , vol.90 , pp. 1679-1684
    • Frische, S.1    Bruno, S.2    Fago, A.3    Weber, R.E.4    Mozzarelli, A.5
  • 32
    • 0018377107 scopus 로고
    • Functional studies on the separated hemoglobin components of an air-breathing catfish Hoplosternum littorate (Hancock)
    • R.L. Garlick, H.F. Bunn, H.J. Fyhn, U.E.H. Fyhn, J.P. Martin, R.W. Noble, and D. Powers Functional studies on the separated hemoglobin components of an air-breathing catfish Hoplosternum littorate (Hancock) Comp. Biochem. Physiol. 62A 1979 219 226
    • (1979) Comp. Biochem. Physiol. , vol.62 , pp. 219-226
    • Garlick, R.L.1    Bunn, H.F.2    Fyhn, H.J.3    Fyhn, U.E.H.4    Martin, J.P.5    Noble, R.W.6    Powers, D.7
  • 33
    • 0042170141 scopus 로고    scopus 로고
    • Neuroprotection and the role of neuroglobin
    • D.J. Garry, and P.P.A. Mammen Neuroprotection and the role of neuroglobin Lancet 362 2003 342 343
    • (2003) Lancet , vol.362 , pp. 342-343
    • Garry, D.J.1    Mammen, P.P.A.2
  • 36
    • 0032495529 scopus 로고    scopus 로고
    • Reactions between nitric oxide and haemoglobin under physiological conditions
    • A.J. Gow, and J.S. Stamler Reactions between nitric oxide and haemoglobin under physiological conditions Nature 391 1998 169 173
    • (1998) Nature , vol.391 , pp. 169-173
    • Gow, A.J.1    Stamler, J.S.2
  • 38
    • 84886639405 scopus 로고
    • Stereochemistry of ATP and GTP bound to fish haemoglobins. a transferred nuclear overhauser enhancement, 31P-nuclear magnetic resonance, oxygen equilibrium and molecular modelling study
    • A.M. Gronenborn, G.M. Clore, M. Brunori, B. Giardina, G. Falcioni, and M.F. Perutz Stereochemistry of ATP and GTP bound to fish haemoglobins. A transferred nuclear overhauser enhancement, 31P-nuclear magnetic resonance, oxygen equilibrium and molecular modelling study J. Mol. Biol. 178 1984 731 742
    • (1984) J. Mol. Biol. , vol.178 , pp. 731-742
    • Gronenborn, A.M.1    Clore, G.M.2    Brunori, M.3    Giardina, B.4    Falcioni, G.5    Perutz, M.F.6
  • 40
    • 0037188533 scopus 로고    scopus 로고
    • Nitric oxide reaction with red blood cells and hemoglobin under heterogeneous conditions
    • T.H. Han, D.R. Hyduke, M.W. Vaughn, J.M. Fukuto, and J.C. Liao Nitric oxide reaction with red blood cells and hemoglobin under heterogeneous conditions PNAS 99 2002 7763 7768
    • (2002) PNAS , vol.99 , pp. 7763-7768
    • Han, T.H.1    Hyduke, D.R.2    Vaughn, M.W.3    Fukuto, J.M.4    Liao, J.C.5
  • 41
    • 0001636393 scopus 로고    scopus 로고
    • The evolution of hemoglobin
    • R. Hardison The evolution of hemoglobin Am. Scient. 87 1999 126 137
    • (1999) Am. Scient. , vol.87 , pp. 126-137
    • Hardison, R.1
  • 42
    • 34548520171 scopus 로고    scopus 로고
    • The 2.7 a crystal structure of deoxygenated hemoglobin from the sea lamprey (Petromyzon marinus): Structural basis for a lowered oxygen affinity and Bohr effect
    • H.A. Heaslet, and W.E. Royer Jr. The 2.7 A crystal structure of deoxygenated hemoglobin from the sea lamprey (Petromyzon marinus): structural basis for a lowered oxygen affinity and Bohr effect Structure 7 1999 517 526
    • (1999) Structure , vol.7 , pp. 517-526
    • Heaslet, H.A.1    Royer Jr., W.E.2
  • 43
  • 44
    • 0023988604 scopus 로고
    • High altitude respiration of birds structural adaptations in the major and minor hemoglobin components of adult Ruppell's griffon (Gyps ruepellii Aegypiinae): A new molecular pattern for hypoxic tolerance
    • I. Hiebl, R.E. Weber, D. Schneeganss, J. Kösters, and G. Braunitzer High altitude respiration of birds structural adaptations in the major and minor hemoglobin components of adult Ruppell's griffon (Gyps ruepellii Aegypiinae): a new molecular pattern for hypoxic tolerance Biol. Chem. Hoppe-Seyler 369 1988 217 232
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 217-232
    • Hiebl, I.1    Weber, R.E.2    Schneeganss, D.3    Kösters, J.4    Braunitzer, G.5
  • 48
    • 0242322032 scopus 로고    scopus 로고
    • Allosteric effect of water in fish and human hemoglobins
    • C. Hundahl, A. Fago, H. Malte, and R.E. Weber Allosteric effect of water in fish and human hemoglobins J. Biol. Chem. 278 2003 42769 42773
    • (2003) J. Biol. Chem. , vol.278 , pp. 42769-42773
    • Hundahl, C.1    Fago, A.2    Malte, H.3    Weber, R.E.4
  • 49
    • 0017138267 scopus 로고
    • Aquatic life at high altitude: Respiratory adaptations in the Lake Titicaca frog Telmatobius culeus
    • V.H. Hutchison, H.B. Haines, and G. Engbretson Aquatic life at high altitude: respiratory adaptations in the Lake Titicaca frog Telmatobius culeus Respir. Physiol. 27 1976 115 129
    • (1976) Respir. Physiol. , vol.27 , pp. 115-129
    • Hutchison, V.H.1    Haines, H.B.2    Engbretson, G.3
  • 50
    • 0023505509 scopus 로고
    • Endothelium-derived relaxing factor produced and released from artery and vein is nitric-oxide
    • L.J. Ignarro, G.M. Buga, K.S. Wood, R.E. Byrns, and G. Chaudhuri Endothelium-derived relaxing factor produced and released from artery and vein is nitric-oxide Proc. Natl. Acad. Sci. U.S.A. 84 1987 9265 9269
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 9265-9269
    • Ignarro, L.J.1    Buga, G.M.2    Wood, K.S.3    Byrns, R.E.4    Chaudhuri, G.5
  • 51
    • 0021104746 scopus 로고
    • Oxygen equilibrium studies on hemoglobin from the bluefin tuna (Thunnus thynnus)
    • M. Ikeda-Saito, T. Yonetani, and Q.H. Gibson Oxygen equilibrium studies on hemoglobin from the bluefin tuna (Thunnus thynnus) J. Mol. Biol. 168 1983 673 686
    • (1983) J. Mol. Biol. , vol.168 , pp. 673-686
    • Ikeda-Saito, M.1    Yonetani, T.2    Gibson, Q.H.3
  • 53
    • 0028981025 scopus 로고
    • Structure of deoxyhaemoglobin of the Antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the Root effect by comparison of the liganded and unliganded haemoglobin structures
    • N. Ito, N.H. Komiyama, and G. Fermi Structure of deoxyhaemoglobin of the Antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the Root effect by comparison of the liganded and unliganded haemoglobin structures J. Mol. Biol. 250 1995 648 658
    • (1995) J. Mol. Biol. , vol.250 , pp. 648-658
    • Ito, N.1    Komiyama, N.H.2    Fermi, G.3
  • 54
    • 0023077250 scopus 로고
    • Thermodynamic analysis of precisely measured oxygen equilibria of tench hemoglobin and their dependence on ATP and protons
    • F.B. Jensen, and R.E. Weber Thermodynamic analysis of precisely measured oxygen equilibria of tench hemoglobin and their dependence on ATP and protons J. Comp. Physiol. 157B 1987 137 143
    • (1987) J. Comp. Physiol. , vol.157 , pp. 137-143
    • Jensen, F.B.1    Weber, R.E.2
  • 56
    • 0032190855 scopus 로고    scopus 로고
    • Interaction between haemoglobin and synthetic peptides of the N-terminal cytoplasmic fragment of trout band 3 (AE1) protein
    • F.B. Jensen, M.H. Jakobsen, and R.E. Weber Interaction between haemoglobin and synthetic peptides of the N-terminal cytoplasmic fragment of trout band 3 (AE1) protein J. Exp. Biol. 201 1998 2685 2690
    • (1998) J. Exp. Biol. , vol.201 , pp. 2685-2690
    • Jensen, F.B.1    Jakobsen, M.H.2    Weber, R.E.3
  • 57
    • 0037406633 scopus 로고    scopus 로고
    • Nitrite disrupts multiple physiological functions in aquatic animals
    • F.B. Jensen Nitrite disrupts multiple physiological functions in aquatic animals Comp. Biochem. Physiol. A: Mol. Integr. Physiol. 135 2003 9 24
    • (2003) Comp. Biochem. Physiol. A: Mol. Integr. Physiol. , vol.135 , pp. 9-24
    • Jensen, F.B.1
  • 58
    • 0026095651 scopus 로고
    • Adaptation of bird hemoglobins to high altitudes: Demonstration of molecular mechanism by protein engineering
    • T.-H. Jessen, R.E. Weber, G. Fermi, J. Tame, and G. Braunitzer Adaptation of bird hemoglobins to high altitudes: demonstration of molecular mechanism by protein engineering Proc. Natl. Acad. Sci. U.S.A. 88 1991 6519 6522
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 6519-6522
    • Jessen, T.-H.1    Weber, R.E.2    Fermi, G.3    Tame, J.4    Braunitzer, G.5
  • 59
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin: A dynamic activity of blood involved in vascular control
    • L. Jia, C. Bonaventura, J. Bonaventura, and J.S. Stamler S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control Nature 380 1996 221 226
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 60
    • 0003121594 scopus 로고
    • 2 affinity associated with air breathing in osteoglossid fishes
    • 2 affinity associated with air breathing in osteoglossid fishes Can. J. Zool. 56 1978 891 897
    • (1978) Can. J. Zool. , vol.56 , pp. 891-897
    • Johansen, K.1    Mangum, C.P.2    Weber, R.E.3
  • 62
    • 0023811996 scopus 로고
    • Oxygen binding properties, capillary densities and heart weights in high altitude camelids
    • K.D. Jürgens, M. Pietschmann, K. Yamaguchi, and T. Kleinschmidt Oxygen binding properties, capillary densities and heart weights in high altitude camelids J. Comp. Physiol. B 158 1988 469 477
    • (1988) J. Comp. Physiol. B , vol.158 , pp. 469-477
    • Jürgens, K.D.1    Pietschmann, M.2    Yamaguchi, K.3    Kleinschmidt, T.4
  • 64
    • 0018544480 scopus 로고
    • The neutral theory of molecular evolution
    • M. Kimura The neutral theory of molecular evolution Sci. Am. 241 1979 94 104
    • (1979) Sci. Am. , vol.241 , pp. 94-104
    • Kimura, M.1
  • 65
    • 0022668360 scopus 로고
    • Interaction of allosteric effectors with a-globin chains and high altitude respiration in mammals. the primary structure of two tylopod hemoglobins with high oxygen affinity: Vicuna (Lama vicugna) and alpaca (Lama pacos)
    • T. Kleinschmidt, J. März, K.D. Jürgens, and G. Braunitzer Interaction of allosteric effectors with a-globin chains and high altitude respiration in mammals. The primary structure of two tylopod hemoglobins with high oxygen affinity: vicuna (Lama vicugna) and alpaca (Lama pacos) Biol. Chem. Hoppe-Seyler 367 1986 153 160
    • (1986) Biol. Chem. Hoppe-Seyler , vol.367 , pp. 153-160
    • Kleinschmidt, T.1    März, J.2    Jürgens, K.D.3    Braunitzer, G.4
  • 66
  • 67
    • 0028852689 scopus 로고
    • Transplanting a unique allosteric effect from crocodile into human haemoglobin
    • N.H. Komiyama, G. Miyazaki, J. Tame, and K. Nagai Transplanting a unique allosteric effect from crocodile into human haemoglobin Nature 373 1995 244 246
    • (1995) Nature , vol.373 , pp. 244-246
    • Komiyama, N.H.1    Miyazaki, G.2    Tame, J.3    Nagai, K.4
  • 68
    • 0022552863 scopus 로고
    • Extended oxygen delivery from the nerve hemoglobin of Tellina alternata (Bivalvia)
    • D.W. Kraus, and J.M. Colacino Extended oxygen delivery from the nerve hemoglobin of Tellina alternata (Bivalvia) Science 232 1986 90 92
    • (1986) Science , vol.232 , pp. 90-92
    • Kraus, D.W.1    Colacino, J.M.2
  • 70
    • 0027422080 scopus 로고
    • The effect of 75% glycerol on the oxygen binding properties of carp hemoglobin
    • L.D. Kwiatkowski, and R.W. Noble The effect of 75% glycerol on the oxygen binding properties of carp hemoglobin Biochem. Biophys. Res. Commun. 195 1993 1218 1223
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 1218-1223
    • Kwiatkowski, L.D.1    Noble, R.W.2
  • 71
    • 0042232406 scopus 로고    scopus 로고
    • ATP induced reverse temperature effect in iso-hemoglobins from the endothermic porbeagle shark (Lamna nasus)
    • C. Larsen, H. Malte, and R.E. Weber ATP induced reverse temperature effect in iso-hemoglobins from the endothermic porbeagle shark (Lamna nasus) J. Biol. Chem. 278 2003 30741 30747
    • (2003) J. Biol. Chem. , vol.278 , pp. 30741-30747
    • Larsen, C.1    Malte, H.2    Weber, R.E.3
  • 72
    • 0014083461 scopus 로고
    • Respiratory adaptations in selected amphibians
    • C. Lenfant, and K. Johansen Respiratory adaptations in selected amphibians Respir. Physiol. 2 1967 247 260
    • (1967) Respir. Physiol. , vol.2 , pp. 247-260
    • Lenfant, C.1    Johansen, K.2
  • 73
    • 0035850791 scopus 로고    scopus 로고
    • The crystal structure of bar-headed goose hemoglobin in deoxy form: The allosteric mechanism of a hemoglobin species with high oxygen affinity
    • Y. Liang, Z. Hua, X. Liang, Q. Xu, and G. Lu The crystal structure of bar-headed goose hemoglobin in deoxy form: the allosteric mechanism of a hemoglobin species with high oxygen affinity J. Mol. Biol. 313 2001 123 137
    • (2001) J. Mol. Biol. , vol.313 , pp. 123-137
    • Liang, Y.1    Hua, Z.2    Liang, X.3    Xu, Q.4    Lu, G.5
  • 74
    • 0023621164 scopus 로고
    • X-ray crystallographic and functional studies of human haemoglobin mutants produced in Escherichia coli
    • B.F. Luisi, K. Nagai, M. Perutz, and M.F. Perutz X-ray crystallographic and functional studies of human haemoglobin mutants produced in Escherichia coli Acta Haematol. 78 1987 85 89
    • (1987) Acta Haematol. , vol.78 , pp. 85-89
    • Luisi, B.F.1    Nagai, K.2    Perutz, M.3    Perutz, M.F.4
  • 75
    • 0016642727 scopus 로고
    • Functional properties of hemoglobins in the teleost Tilapia grahami
    • G. Lykkeboe, K. Johansen, and G.M.O. Maloiy Functional properties of hemoglobins in the teleost Tilapia grahami J. Comp. Physiol. 104 1975 1 11
    • (1975) J. Comp. Physiol. , vol.104 , pp. 1-11
    • Lykkeboe, G.1    Johansen, K.2    Maloiy, G.M.O.3
  • 76
    • 0019130296 scopus 로고
    • Oxygen equilibria of ectotherm blood containing mutliple hemoglobins
    • L.A. Maginniss, Y.K. Song, and R.B. Reeves Oxygen equilibria of ectotherm blood containing mutliple hemoglobins Respir. Physiol. 42 1980 329 343
    • (1980) Respir. Physiol. , vol.42 , pp. 329-343
    • Maginniss, L.A.1    Song, Y.K.2    Reeves, R.B.3
  • 78
    • 0034595830 scopus 로고    scopus 로고
    • Functional coupling of oxygen binding and vasoactivity in S-nitrosohemoglobin
    • T.J. McMahon, S.A. Exton, J. Bonaventura, D.J. Singel, and S.J. Solomon Functional coupling of oxygen binding and vasoactivity in S-nitrosohemoglobin J. Biol. Chem. 275 2000 16738 16745
    • (2000) J. Biol. Chem. , vol.275 , pp. 16738-16745
    • McMahon, T.J.1    Exton, S.A.2    Bonaventura, J.3    Singel, D.J.4    Solomon, S.J.5
  • 80
    • 0037077231 scopus 로고    scopus 로고
    • Crystal structures of deoxy- and carbonmonoxyhemoglobin F1 from the hagfish Eptatretus burgeri
    • M. Mito, K.T. Chong, G. Miyazaki, S. Adachi, S.Y. Park, J.R.H. Tame, and H. Morimoto Crystal structures of deoxy- and carbonmonoxyhemoglobin F1 from the hagfish Eptatretus burgeri J. Biol. Chem. 277 2002 21898 21905
    • (2002) J. Biol. Chem. , vol.277 , pp. 21898-21905
    • Mito, M.1    Chong, K.T.2    Miyazaki, G.3    Adachi, S.4    Park, S.Y.5    Tame, J.R.H.6    Morimoto, H.7
  • 81
    • 0025883342 scopus 로고
    • Nitric-oxide - Physiology, pathophysiology, and pharmacology
    • S. Moncada, R.M.J. Palmer, and E.A. Higgs Nitric-oxide - physiology, pathophysiology, and pharmacology Pharmacol. Rev. 43 1991 109 142
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.J.2    Higgs, E.A.3
  • 82
    • 0038035496 scopus 로고    scopus 로고
    • Water regulates oxygen binding in hagfish (Myxine glutinosa) hemoglobin
    • G. Müller, A. Fago, and R.E. Weber Water regulates oxygen binding in hagfish (Myxine glutinosa) hemoglobin J. Exp. Biol. 206 2003 1389 1395
    • (2003) J. Exp. Biol. , vol.206 , pp. 1389-1395
    • Müller, G.1    Fago, A.2    Weber, R.E.3
  • 84
    • 0344443777 scopus 로고    scopus 로고
    • Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin mediated nitrite reduction
    • E.N. Nagababu, S. Ramasamy, D.R. Abernethy, and J.M. Rifkind Active nitric oxide produced in the red cell under hypoxic conditions by deoxyhemoglobin mediated nitrite reduction J. Biol. Chem. 278 2003 46349 46356
    • (2003) J. Biol. Chem. , vol.278 , pp. 46349-46356
    • Nagababu, E.N.1    Ramasamy, S.2    Abernethy, D.R.3    Rifkind, J.M.4
  • 86
    • 0026451383 scopus 로고
    • Inhibition of adrenergic proton extrusion in rainbow trout red cells by nitrite-induced methaemoglobinaemia
    • M. Nikinmaa, and F.B. Jensen Inhibition of adrenergic proton extrusion in rainbow trout red cells by nitrite-induced methaemoglobinaemia J. Comp. Physiol. B 162 1992 424 429
    • (1992) J. Comp. Physiol. B , vol.162 , pp. 424-429
    • Nikinmaa, M.1    Jensen, F.B.2
  • 87
    • 0027458791 scopus 로고
    • Haemoglobin function in intact Lampetra fluviatilis erythrocytes
    • M. Nikinmaa Haemoglobin function in intact Lampetra fluviatilis erythrocytes Respir. Physiol. 91 1993 283 293
    • (1993) Respir. Physiol. , vol.91 , pp. 283-293
    • Nikinmaa, M.1
  • 88
    • 0023055084 scopus 로고
    • Functional properties of hemoglobins from deep-sea fish: Correlations with depth distribution and presence of a swimbladder
    • R.W. Noble, L.D. Kwiatkowski, A. De Young, B.J. Davis, R.L. Haedrich, L.-T. Tam, and A.F. Riggs Functional properties of hemoglobins from deep-sea fish: correlations with depth distribution and presence of a swimbladder Biochim. Biophys. Acta 870 1986 552 563
    • (1986) Biochim. Biophys. Acta , vol.870 , pp. 552-563
    • Noble, R.W.1    Kwiatkowski, L.D.2    De Young, A.3    Davis, B.J.4    Haedrich, R.L.5    Tam, L.-T.6    Riggs, A.F.7
  • 89
    • 0018406467 scopus 로고
    • Oxygen dissociation constants in haemoglobins of Helicops modestus and Liophis miliaris, two water-snakes with different morphological adaptations to their aquatic environment
    • S.H. Ogo, A.S. Abe, and A. Focesi Jr. Oxygen dissociation constants in haemoglobins of Helicops modestus and Liophis miliaris, two water-snakes with different morphological adaptations to their aquatic environment Comp. Biochem. Physiol. A 63A 1979 285 289
    • (1979) Comp. Biochem. Physiol. a , vol.63 , pp. 285-289
    • Ogo, S.H.1    Abe, A.S.2    Focesi Jr., A.3
  • 90
    • 0012278832 scopus 로고
    • Content of organic polyphosphates and their allosteric effects on haemoglobins from the water-snakes Helicops modestus and Liophis miliaris
    • S.H. Ogo, M.S.A. Matsuura, and A. Focesi Jr. Content of organic polyphosphates and their allosteric effects on haemoglobins from the water-snakes Helicops modestus and Liophis miliaris Comp. Biochem. Physiol. A 78A 1984 587 589
    • (1984) Comp. Biochem. Physiol. a , vol.78 , pp. 587-589
    • Ogo, S.H.1    Matsuura, M.S.A.2    Focesi Jr., A.3
  • 91
  • 93
    • 1242277881 scopus 로고    scopus 로고
    • The Root effect - A physiological perspective
    • B. Pelster, and H. Decker The Root effect - a physiological perspective Micron 35 2004 73 74
    • (2004) Micron , vol.35 , pp. 73-74
    • Pelster, B.1    Decker, H.2
  • 94
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin haem-haem interaction and the problem of allostery
    • M.F. Perutz Stereochemistry of cooperative effects in haemoglobin haem-haem interaction and the problem of allostery Nature 228 1970 726 734
    • (1970) Nature , vol.228 , pp. 726-734
    • Perutz, M.F.1
  • 95
    • 0018654083 scopus 로고
    • Regulation of oxygen affinity of hemoglobin: Influence of structure of the globin on the heme iron
    • M.F. Perutz Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron Ann. Rev. Biochem. 48 1979 327 386
    • (1979) Ann. Rev. Biochem. , vol.48 , pp. 327-386
    • Perutz, M.F.1
  • 96
    • 0018860147 scopus 로고
    • Regulation of oxygen affinity of mammalian haemoglobins
    • M.F. Perutz, and K. Imai Regulation of oxygen affinity of mammalian haemoglobins J. Mol. Biol. 136 1980 183 191
    • (1980) J. Mol. Biol. , vol.136 , pp. 183-191
    • Perutz, M.F.1    Imai, K.2
  • 97
    • 0019964409 scopus 로고
    • Stereochemistry of cooperative effects in fish and amphibian haemoglobins
    • M.F. Perutz, and M. Brunori Stereochemistry of cooperative effects in fish and amphibian haemoglobins Nature 299 5882 1982 421 426
    • (1982) Nature , vol.299 , Issue.5882 , pp. 421-426
    • Perutz, M.F.1    Brunori, M.2
  • 98
    • 0021004799 scopus 로고
    • Species adaptation in a protein molecule
    • M.F. Perutz Species adaptation in a protein molecule Mol. Biol. Evol. 1 1 1983 1 28
    • (1983) Mol. Biol. Evol. , vol.1 , Issue.1 , pp. 1-28
    • Perutz, M.F.1
  • 99
    • 0028245286 scopus 로고
    • The chloride effect in human haemoglobin a new kind of allosteric mechanism
    • M.F. Perutz, D.T. Shih, and D. Williamson The chloride effect in human haemoglobin A new kind of allosteric mechanism J. Mol. Biol. 239 1994 555 560
    • (1994) J. Mol. Biol. , vol.239 , pp. 555-560
    • Perutz, M.F.1    Shih, D.T.2    Williamson, D.3
  • 102
    • 0025073712 scopus 로고
    • Primary structure and oxygen-binding properties of the hemoglobin from guanaco (Lama guanacoe, Tylopoda)
    • M. Piccinini, T. Kleinschmidt, K.D. Jürgens, and G. Braunitzer Primary structure and oxygen-binding properties of the hemoglobin from guanaco (Lama guanacoe, Tylopoda) Biol. Chem. Hoppe Seyler 371 1990 641 648
    • (1990) Biol. Chem. Hoppe Seyler , vol.371 , pp. 641-648
    • Piccinini, M.1    Kleinschmidt, T.2    Jürgens, K.D.3    Braunitzer, G.4
  • 103
    • 0022555544 scopus 로고
    • The role of catecholamines in erythrocyte pH regulation and oxygen transport in rainbow trout (Salmo gairdneri) during exercise
    • D.R.N. Primmett, D.J. Randall, M. Mazeaud, and R.G. Boutilier The role of catecholamines in erythrocyte pH regulation and oxygen transport in rainbow trout (Salmo gairdneri) during exercise J. Exp. Biol. 122 1986 139 148
    • (1986) J. Exp. Biol. , vol.122 , pp. 139-148
    • Primmett, D.R.N.1    Randall, D.J.2    Mazeaud, M.3    Boutilier, R.G.4
  • 106
    • 0022841820 scopus 로고
    • High sulfhydryl content in turtle erythrocytes: Is there a relation with resistance to hypoxia?
    • E. Reischl High sulfhydryl content in turtle erythrocytes: is there a relation with resistance to hypoxia? Comp. Biochem. Physiol. B 85 1986 723 726
    • (1986) Comp. Biochem. Physiol. B , vol.85 , pp. 723-726
    • Reischl, E.1
  • 107
    • 36949090402 scopus 로고
    • Oxygen equilibrium of hæmoglobin from Thunnus thynnus
    • A. Rossi-Fanelli, E. Antonini, and R. Giuffrè Oxygen equilibrium of hæmoglobin from Thunnus thynnus Nature 186 1960 895 897
    • (1960) Nature , vol.186 , pp. 895-897
    • Rossi-Fanelli, A.1    Antonini, E.2    Giuffrè, R.3
  • 108
    • 0024854847 scopus 로고
    • The 2.4 Å crystal structure of Scapharca dimeric hemoglobin. Cooperativity based on directly communicating hemes at a novel subunit
    • W.E. Royer Jr., W.A. Hendrickson, and E. Chiancone The 2.4 Å crystal structure of Scapharca dimeric hemoglobin. Cooperativity based on directly communicating hemes at a novel subunit J. Biol. Chem. 264 1989 21052 21061
    • (1989) J. Biol. Chem. , vol.264 , pp. 21052-21061
    • Royer Jr., W.E.1    Hendrickson, W.A.2    Chiancone, E.3
  • 110
    • 0035336687 scopus 로고    scopus 로고
    • Cooperative hemoglobins: Conserved fold, diverse quaternary assemblies and allosteric mechanisms
    • W.E. Royer Jr., J.E. Knapp, K. Strand, and H.A. Heaslet Cooperative hemoglobins: conserved fold, diverse quaternary assemblies and allosteric mechanisms Trends Biochem. Sci. 26 2001 297 304
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 297-304
    • Royer Jr., W.E.1    Knapp, J.E.2    Strand, K.3    Heaslet, H.A.4
  • 112
    • 0038380918 scopus 로고
    • Some hybrids of deoxygenated sea lamprey hemoglobins (Petromyzon marinus)
    • N.M. Rumen, and W.E. Love Some hybrids of deoxygenated sea lamprey hemoglobins (Petromyzon marinus) Acta Chem. Scand. 17 1963 S222 S225
    • (1963) Acta Chem. Scand. , vol.17
    • Rumen, N.M.1    Love, W.E.2
  • 113
  • 115
    • 0022469426 scopus 로고
    • Multiple hemoglobins of the cutthroat trout Salmo clarki
    • J.N. Southard, C.R. Berry, and T.M. Farley Multiple hemoglobins of the cutthroat trout Salmo clarki J. Exp. Zool. 239 1986 7 16
    • (1986) J. Exp. Zool. , vol.239 , pp. 7-16
    • Southard, J.N.1    Berry, C.R.2    Farley, T.M.3
  • 117
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation: The prototypic redox-based signaling mechanism
    • J.S. Stamler, S. Lamas, and F.C. Fang Nitrosylation: the prototypic redox-based signaling mechanism Cell 106 2001 675 683
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 118
  • 119
    • 0021361429 scopus 로고
    • Oxygen binding and aggregation of bullfrog hemoglobin
    • L.-T. Tam, and A.F. Riggs Oxygen binding and aggregation of bullfrog hemoglobin J. Biol. Chem. 259 1984 2610 2616
    • (1984) J. Biol. Chem. , vol.259 , pp. 2610-2616
    • Tam, L.-T.1    Riggs, A.F.2
  • 120
    • 0026586178 scopus 로고
    • The amino acid sequence and oxygen-binding properties of the single hemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps
    • M. Tamburrini, A. Brancaccio, R. Ippoliti, and G. Di Prisco The amino acid sequence and oxygen-binding properties of the single hemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps Arch. Biochem. Biophys. 292 1992 295 302
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 295-302
    • Tamburrini, M.1    Brancaccio, A.2    Ippoliti, R.3    Di Prisco, G.4
  • 121
    • 8844273048 scopus 로고    scopus 로고
    • Haemoglobin with a(l)titude
    • J. Tame Haemoglobin with a(l)titude J. Exp. Biol. 206 2003 1105
    • (2003) J. Exp. Biol. , vol.206 , pp. 1105
    • Tame, J.1
  • 122
    • 0031280469 scopus 로고    scopus 로고
    • Oxygen-binding properties of total hemoglobin and isolated components of the terrestrial tortoise Geochelone carbonaria
    • M.A. Torsoni, R.I. Viana, G.R. Stoppa, M. Cesquini, B.F. Barros, and S.H. Ogo Oxygen-binding properties of total hemoglobin and isolated components of the terrestrial tortoise Geochelone carbonaria Comp. Biochem. Physiol. A 118 1997 679 684
    • (1997) Comp. Biochem. Physiol. a , vol.118 , pp. 679-684
    • Torsoni, M.A.1    Viana, R.I.2    Stoppa, G.R.3    Cesquini, M.4    Barros, B.F.5    Ogo, S.H.6
  • 123
    • 0037205447 scopus 로고    scopus 로고
    • A ubiquitously expressed human hexacoordinate hemoglobin
    • J.T. Trent, and M.S. Hargrove A ubiquitously expressed human hexacoordinate hemoglobin J. Biol. Chem. 277 2002 19538 19545
    • (2002) J. Biol. Chem. , vol.277 , pp. 19538-19545
    • Trent, J.T.1    Hargrove, M.S.2
  • 125
    • 0031859924 scopus 로고    scopus 로고
    • Estimation of nitric oxide production and reaction rates in tissue by use of a mathematical model
    • M.W. Vaughn, L. Kuo, and J.C. Liao Estimation of nitric oxide production and reaction rates in tissue by use of a mathematical model Am. J. Physiol.-Heart Circul. Physiol. 43 1998 H2163 H2176
    • (1998) Am. J. Physiol.-Heart Circul. Physiol. , vol.43
    • Vaughn, M.W.1    Kuo, L.2    Liao, J.C.3
  • 126
    • 0036915028 scopus 로고    scopus 로고
    • Haemoglobin from microorganism to man: A single protein folding, a variety of functions
    • H. Wajcman, and L. Kiger Haemoglobin from microorganism to man: a single protein folding, a variety of functions Comptes Rendus Biol. 325 2002 1159 1174
    • (2002) Comptes Rendus Biol. , vol.325 , pp. 1159-1174
    • Wajcman, H.1    Kiger, L.2
  • 128
    • 0016742745 scopus 로고
    • Hemoglobins of the tadpole of the bullfrog Rana catesbeiana. Structure and function of isolated components
    • K.W.K. Watt, and A. Riggs Hemoglobins of the tadpole of the bullfrog Rana catesbeiana. Structure and function of isolated components J. Biol. Chem. 250 1975 5934 5944
    • (1975) J. Biol. Chem. , vol.250 , pp. 5934-5944
    • Watt, K.W.K.1    Riggs, A.2
  • 129
    • 0019313853 scopus 로고
    • Hemoglobins of the tadpole of the bullfrog Rana catesbeiana. Amino acid sequence of the beta chain of a major component
    • K.W. Watt, T. Maruyama, and A. Riggs Hemoglobins of the tadpole of the bullfrog Rana catesbeiana. Amino acid sequence of the beta chain of a major component J. Biol. Chem. 255 1980 3294 3301
    • (1980) J. Biol. Chem. , vol.255 , pp. 3294-3301
    • Watt, K.W.1    Maruyama, T.2    Riggs, A.3
  • 130
    • 0017230736 scopus 로고
    • Physiological properties of eel haemoglobin: Hypoxic acclimation, phosphate effects and multiplicity
    • R.E. Weber, G. Lykkeboe, and K. Johansen Physiological properties of eel haemoglobin: hypoxic acclimation, phosphate effects and multiplicity J. Exp. Biol. 64 1976 75 88
    • (1976) J. Exp. Biol. , vol.64 , pp. 75-88
    • Weber, R.E.1    Lykkeboe, G.2    Johansen, K.3
  • 131
    • 0022982116 scopus 로고
    • Oxygen binding in alligator blood related to temperature, diving and "alkaline tide"
    • R.E. Weber, and F.N. White Oxygen binding in alligator blood related to temperature, diving and "alkaline tide" Am. J. Physiol. 20 1986 R901 R908
    • (1986) Am. J. Physiol. , vol.20
    • Weber, R.E.1    White, F.N.2
  • 132
    • 0023087231 scopus 로고
    • Analysis of teleost hemoglobin by Adair and Monod-Wyman-Changeux models. Effects of nucleoside triphosphates and pH on oxygenation of tench hemoglobin
    • R.E. Weber, F.B. Jensen, and R.P. Cox Analysis of teleost hemoglobin by Adair and Monod-Wyman-Changeux models. Effects of nucleoside triphosphates and pH on oxygenation of tench hemoglobin J. Comp. Physiol. 157B 1987 145 152
    • (1987) J. Comp. Physiol. , vol.157 , pp. 145-152
    • Weber, R.E.1    Jensen, F.B.2    Cox, R.P.3
  • 133
    • 0023993308 scopus 로고
    • High altitude and hemoglobin function in the vultures Gyps rueppelli and Aegypius monachus
    • R.E. Weber, I. Hiebl, and G. Braunitzer High altitude and hemoglobin function in the vultures Gyps rueppelli and Aegypius monachus Biol. Chem. Hoppe-Seyler 369 1988 233 240
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 233-240
    • Weber, R.E.1    Hiebl, I.2    Braunitzer, G.3
  • 136
    • 0028038635 scopus 로고
    • Chloride-dependent organic phosphate sensitivity of the oxygenation reaction in crocodilian hemoglobins
    • R.E. Weber, and F.N. White Chloride-dependent organic phosphate sensitivity of the oxygenation reaction in crocodilian hemoglobins J. Exp. Biol. 192 1994 1 11
    • (1994) J. Exp. Biol. , vol.192 , pp. 1-11
    • Weber, R.E.1    White, F.N.2
  • 140
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • R.E. Weber, and S.N. Vinogradov Nonvertebrate hemoglobins: functions and molecular adaptations Physiol. Rev. 81 2001 569 628
    • (2001) Physiol. Rev. , vol.81 , pp. 569-628
    • Weber, R.E.1    Vinogradov, S.N.2
  • 142
    • 0042928294 scopus 로고    scopus 로고
    • Hemoglobin function in deep-sea and hydrothermal-vent endemic fish: Symenchelis parasitica (Anguillidae) andThermarces cerberus (Zoarcidae)
    • R.E. Weber, S. Hourdez, F. Knowles, and F. Lallier Hemoglobin function in deep-sea and hydrothermal-vent endemic fish: Symenchelis parasitica (Anguillidae) andThermarces cerberus (Zoarcidae) J. Exp. Biol. 206 2003 2693
    • (2003) J. Exp. Biol. , vol.206 , pp. 2693
    • Weber, R.E.1    Hourdez, S.2    Knowles, F.3    Lallier, F.4
  • 143
    • 1242277872 scopus 로고    scopus 로고
    • 'Novel' factors that regulate oxygen binding in vertebrate hemoglobins
    • R.E. Weber, and W. Voelter 'Novel' factors that regulate oxygen binding in vertebrate hemoglobins Micron 35 2004 45 46
    • (2004) Micron , vol.35 , pp. 45-46
    • Weber, R.E.1    Voelter, W.2
  • 144
    • 3242773687 scopus 로고    scopus 로고
    • Modulation of red cell glycolysis: Interactions between vertebrate hemoglobins and cytoplasmic domains of Band 3 red cell membrane proteins
    • R.E. Weber, W. Voelter, A. Fago, H. Echner, E. Campanella, and P.S. Low Modulation of red cell glycolysis: interactions between vertebrate hemoglobins and cytoplasmic domains of Band 3 red cell membrane proteins Am. J. Physiol., Regul. Integr. Comp. Physiol. 287 2004 R454 R464
    • (2004) Am. J. Physiol., Regul. Integr. Comp. Physiol. , vol.287
    • Weber, R.E.1    Voelter, W.2    Fago, A.3    Echner, H.4    Campanella, E.5    Low, P.S.6
  • 145
    • 0017337229 scopus 로고
    • The balance sheet of a hemoglobin. Thermodynamics of CO binding by hemoglobin Trout I
    • J. Wyman, S.J. Gill, L. Noll, B. Giardina, A. Colosimo, and M. Brunori The balance sheet of a hemoglobin. Thermodynamics of CO binding by hemoglobin Trout I J. Mol. Biol. 109 1977 195 205
    • (1977) J. Mol. Biol. , vol.109 , pp. 195-205
    • Wyman, J.1    Gill, S.J.2    Noll, L.3    Giardina, B.4    Colosimo, A.5    Brunori, M.6
  • 146
    • 0141594579 scopus 로고    scopus 로고
    • Measurements of nitric oxide on the heme iron and {beta}-93 thiol of human hemoglobin during cycles of oxygenation and deoxygenation
    • X. Xu, M. Cho, N.Y. Spencer, N. Patel, Z. Huang, H. Shields, S.B. King, M.T. Gladwin, N. Hogg, and D.B. Kim-Shapiro Measurements of nitric oxide on the heme iron and {beta}-93 thiol of human hemoglobin during cycles of oxygenation and deoxygenation PNAS 100 2003 11303 11308
    • (2003) PNAS , vol.100 , pp. 11303-11308
    • Xu, X.1    Cho, M.2    Spencer, N.Y.3    Patel, N.4    Huang, Z.5    Shields, H.6    King, S.B.7    Gladwin, M.T.8    Hogg, N.9    Kim-Shapiro, D.B.10
  • 148
    • 0032729967 scopus 로고    scopus 로고
    • Origin of the suppression of chloride ion sensitivity in human embryonic hemoglobin Gower II
    • T. Zheng, Q. Zhu, and T. Brittain Origin of the suppression of chloride ion sensitivity in human embryonic hemoglobin Gower II IUBMB Life 48 1999 435 437
    • (1999) IUBMB Life , vol.48 , pp. 435-437
    • Zheng, T.1    Zhu, Q.2    Brittain, T.3


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