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Volumn 202, Issue 3, 2011, Pages 549-562

Temperature dependence of haemoglobin-oxygen affinity in heterothermic vertebrates: Mechanisms and biological significance

Author keywords

Haemoglobin; Heterothermy; Oxygen affinity; Oxygen transport; Respiration; Temperature

Indexed keywords

HEMOGLOBIN; OXYGEN;

EID: 80051980772     PISSN: 17481708     EISSN: 17481716     Source Type: Journal    
DOI: 10.1111/j.1748-1716.2010.02204.x     Document Type: Review
Times cited : (63)

References (96)
  • 1
    • 0022108528 scopus 로고
    • The primary structure of hemoglobins from the domestic cat (Felis catus, Felidae)
    • Abbasi, A. & Braunitzer, G. 1985. The primary structure of hemoglobins from the domestic cat (Felis catus, Felidae). Biol Chem Hoppe-Seyler 366, 699-704.
    • (1985) Biol Chem Hoppe-Seyler , vol.366 , pp. 699-704
    • Abbasi, A.1    Braunitzer, G.2
  • 2
    • 0016154360 scopus 로고
    • Calorimetric determination of the heat of oxygenation of human hemoglobin as a function of pH and the extent of reaction
    • Atha, D.H. & Ackers, G.K. 1974. Calorimetric determination of the heat of oxygenation of human hemoglobin as a function of pH and the extent of reaction. Biochemistry 13, 2376-2382.
    • (1974) Biochemistry , vol.13 , pp. 2376-2382
    • Atha, D.H.1    Ackers, G.K.2
  • 3
    • 84912718488 scopus 로고
    • The effect of temperature on the dissociation curve of blood
    • arcroft, J.& King, W.O.R. 1909. The effect of temperature on the dissociation curve of blood. J Physiol (Lond) 39, 374-384.Benesch, R.E., Benesch, R. & Yu, C.I. 1969. The oxygenation of hemoglobin in the presence of 2,3- diphosphoglycerate. Effect of temperature, pH, ionic strength, and hemoglobin concentration. Biochemistry 8, 2567-2571.
    • (1909) J Physiol (Lond) , vol.39 , pp. 374-384
    • Arcroft, J.1    King, W.O.R.2
  • 5
    • 0021891078 scopus 로고
    • Temperature and muscle
    • Bennett, A.F. 1985. Temperature and muscle. J Exp Biol 115, 333-344.
    • (1985) J Exp Biol , vol.115 , pp. 333-344
    • Bennett, A.F.1
  • 6
    • 33750499963 scopus 로고    scopus 로고
    • Evolution of vertebrate haemoglobins: histidine side chains, specific buffer value and Bohr effect
    • Berenbrink, M. 2006. Evolution of vertebrate haemoglobins: histidine side chains, specific buffer value and Bohr effect. Respir Physiol Neurobiol 154, 165-184.
    • (2006) Respir Physiol Neurobiol , vol.154 , pp. 165-184
    • Berenbrink, M.1
  • 7
    • 33748078476 scopus 로고    scopus 로고
    • The uncoupling protein 1 gene (UCP1) is disrupted in the pig lineage: a genetic explanation for poor thermoregulation in piglets
    • Berg, F., Gustafson, U. & Andersson, L. 2006. The uncoupling protein 1 gene (UCP1) is disrupted in the pig lineage: a genetic explanation for poor thermoregulation in piglets. PLoS Genet 2, e129.
    • (2006) PLoS Genet , vol.2 , pp. e129
    • Berg, F.1    Gustafson, U.2    Andersson, L.3
  • 8
    • 0022816822 scopus 로고
    • Structure of the brain and eye heater tissue in marlins, sailfish, and spearfishes
    • Block, B.A. 1986. Structure of the brain and eye heater tissue in marlins, sailfish, and spearfishes. J Morphol 190, 169-189.
    • (1986) J Morphol , vol.190 , pp. 169-189
    • Block, B.A.1
  • 9
    • 0022402788 scopus 로고
    • Warm brain and eye temperatures in sharks
    • Block, B.A. & Carey, F.G. 1985. Warm brain and eye temperatures in sharks. J Comp Physiol [B] 156, 229-236.
    • (1985) J Comp Physiol [B] , vol.156 , pp. 229-236
    • Block, B.A.1    Carey, F.G.2
  • 10
    • 0027231871 scopus 로고
    • Evolution of endothermy in fish: mapping physiological traits on a molecular phylogeny
    • Block, B.A., Finnerty, J.R., Stewart, A.F. & Kidd, J. 1993. Evolution of endothermy in fish: mapping physiological traits on a molecular phylogeny. Science 260, 210-214.
    • (1993) Science , vol.260 , pp. 210-214
    • Block, B.A.1    Finnerty, J.R.2    Stewart, A.F.3    Kidd, J.4
  • 11
    • 84935023004 scopus 로고
    • Ü ber einen in biologischer Beziehung wichtigen Einfluss, den die Kohlensaurespannung des Blutes auf dessen Sauerstoffbindung ubt
    • Bohr, C., Hasselbalch, K. & Krogh, A. 1904. Ü ber einen in biologischer Beziehung wichtigen Einfluss, den die Kohlensaurespannung des Blutes auf dessen Sauerstoffbindung ubt. Skand Arch Physiol 16, 402-412.
    • (1904) Skand Arch Physiol , vol.16 , pp. 402-412
    • Bohr, C.1    Hasselbalch, K.2    Krogh, A.3
  • 13
    • 0030273677 scopus 로고    scopus 로고
    • Effect of haemoglobin oxygenation on Bohr proton release and CO2 excretion in the rainbow trout
    • Brauner, C.J., Gilmour, K.M. & Perry, S.F. 1996. Effect of haemoglobin oxygenation on Bohr proton release and CO2 excretion in the rainbow trout. Respir Physiol 106, 65-70.
    • (1996) Respir Physiol , vol.106 , pp. 65-70
    • Brauner, C.J.1    Gilmour, K.M.2    Perry, S.F.3
  • 15
    • 0009892750 scopus 로고
    • Effects of open- and closedsystem temperature changes on blood oxygen dissociation curves of skipjack tuna, Katsuwonus pelamis, and yellowfin tuna, Thunnus albacares
    • Brill, R.W. & Bushnell, P.G. 1991. Effects of open- and closedsystem temperature changes on blood oxygen dissociation curves of skipjack tuna, Katsuwonus pelamis, and yellowfin tuna, Thunnus albacares. Can J Zool 69, 1814-1821.
    • (1991) Can J Zool , vol.69 , pp. 1814-1821
    • Brill, R.W.1    Bushnell, P.G.2
  • 16
    • 33750973397 scopus 로고    scopus 로고
    • Effects of open- and closedsystem temperature changes on blood O2-binding characteristics of Atlantic bluefin tuna (Thunnus thynnus)
    • Brill, R. & Bushnell, P. 2006. Effects of open- and closedsystem temperature changes on blood O2-binding characteristics of Atlantic bluefin tuna (Thunnus thynnus). Fish Physiol Biochem 32, 283-294.
    • (2006) Fish Physiol Biochem , vol.32 , pp. 283-294
    • Brill, R.1    Bushnell, P.2
  • 19
    • 0024997964 scopus 로고
    • Temperature modulation of oxygen transport in a diving mammal (Balaenoptera acutorostrata)
    • Brix, O., Condò , S.G., Bardgard, A., Tavazzi, B. & Giardina, B. 1990b. Temperature modulation of oxygen transport in a diving mammal (Balaenoptera acutorostrata). Biochem J 271, 509-513.
    • (1990) Biochem J , vol.271 , pp. 509-513
    • Brix, O.1    Condò, S.G.2    Bardgard, A.3    Tavazzi, B.4    Giardina, B.5
  • 20
  • 23
    • 0015575902 scopus 로고
    • Fishes with warm bodies
    • Carey, F.G. 1973. Fishes with warm bodies. Sci Am 228, 36-44.
    • (1973) Sci Am , vol.228 , pp. 36-44
    • Carey, F.G.1
  • 24
    • 0017688691 scopus 로고
    • Reverse temperature dependence of tuna hemoglobin oxygenation
    • Carey, F.G. & Gibson, Q.H. 1977. Reverse temperature dependence of tuna hemoglobin oxygenation. Biochem Biophys Res Com 78, 1376-1382.
    • (1977) Biochem Biophys Res Com , vol.78 , pp. 1376-1382
    • Carey, F.G.1    Gibson, Q.H.2
  • 25
    • 0014444846 scopus 로고
    • Mako and porbeagle - warmbodied sharks
    • Carey, F.G. & Teal, J.M. 1969. Mako and porbeagle - warmbodied sharks. Comp Biochem Physiol 28, 199.
    • (1969) Comp Biochem Physiol , vol.28 , pp. 199
    • Carey, F.G.1    Teal, J.M.2
  • 27
    • 0004760138 scopus 로고
    • Temperatureinduced changes in blood gas equilibria in the albacore, Thunnus alalunga, a warm-bodied tuna
    • Cech, J.J., Laurs, R.M. Jr & Graham, J.B. 1984. Temperatureinduced changes in blood gas equilibria in the albacore, Thunnus alalunga, a warm-bodied tuna. J Exp Biol 109, 21-34.
    • (1984) J Exp Biol , vol.109 , pp. 21-34
    • Cech, J.J.1    Laurs Jr, R.M.2    Graham, J.B.3
  • 28
    • 0014502524 scopus 로고
    • The interaction of organic and inorganic phosphates with hemoglobin
    • Chanutin, A. & Hermann, E. 1969. The interaction of organic and inorganic phosphates with hemoglobin. Arch Biochem Biophys 131, 180-184.
    • (1969) Arch Biochem Biophys , vol.131 , pp. 180-184
    • Chanutin, A.1    Hermann, E.2
  • 30
    • 73949148000 scopus 로고    scopus 로고
    • Reduced and reversed temperature dependence of blood oxygenation in an ectothermic scombrid fish: implications for the evolution of regional heterothermy?
    • Clark, T.D., Rummer, J.L., Sepulveda, C.A., Farrell, A.P. & Brauner, C.J. 2010. Reduced and reversed temperature dependence of blood oxygenation in an ectothermic scombrid fish: implications for the evolution of regional heterothermy? J Comp Physiol B 180, 73-82.
    • (2010) J Comp Physiol , vol.180 B , pp. 73-82
    • Clark, T.D.1    Rummer, J.L.2    Sepulveda, C.A.3    Farrell, A.P.4    Brauner, C.J.5
  • 31
    • 0026579114 scopus 로고
    • A comparative study of the temperature dependence of the oxygen-binding properties of mammalian hemoglobins
    • Coletta, M., Clementi, M.E., Ascenzi, P., Petruzzelli, R., Condò , S.G. & Giardina, B. 1992. A comparative study of the temperature dependence of the oxygen-binding properties of mammalian hemoglobins. Eur J Biochem 204, 1155-1157.
    • (1992) Eur J Biochem , vol.204 , pp. 1155-1157
    • Coletta, M.1    Clementi, M.E.2    Ascenzi, P.3    Petruzzelli, R.4    Condò, S.G.5    Giardina, B.6
  • 35
    • 84911875870 scopus 로고
    • (Stereoroentgenographical studies on peripheral arteries of the anterior and posterior extremities of the bears) - in Japanese
    • Daigo, M., Sato, Y., Otsuka, M., Yoshimura, T., Komyama, S. & Ogawa, Y. 1972. (Stereoroentgenographical studies on peripheral arteries of the anterior and posterior extremities of the bears) - in Japanese. Bull Nippon Vet Zootech Coll 21, 32-40.
    • (1972) Bull Nippon Vet Zootech Coll , vol.21 , pp. 32-40
    • Daigo, M.1    Sato, Y.2    Otsuka, M.3    Yoshimura, T.4    Komyama, S.5    Ogawa, Y.6
  • 36
    • 3042702475 scopus 로고    scopus 로고
    • From the Arctic to fetal life: physiological importance and structural basis of an 'additional' chloridebinding site in haemoglobin
    • De Rosa, M.C., Castagnola, M., Bertonati, C., Galtieri, A. & Giardina, B. 2004. From the Arctic to fetal life: physiological importance and structural basis of an 'additional' chloridebinding 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
  • 37
    • 0002049738 scopus 로고
    • Ü ber die Messung des Blutquantums in den Herzventrikeln
    • Fick, A. 1870. Ü ber die Messung des Blutquantums in den Herzventrikeln. Sitzber Physik Med Ges, WÜ rzburg 2, 16.
    • (1870) Sitzber Physik Med Ges, WÜ rzburg , vol.2 , pp. 16
    • Fick, A.1
  • 38
    • 11844254744 scopus 로고    scopus 로고
    • Warm eyes provide superior vision in swordfishes
    • Fritsches, K.A., Brill, R.W. & Warrant, E.J. 2005. Warm eyes provide superior vision in swordfishes. Curr Biol 15, 55-58.
    • (2005) Curr Biol , vol.15 , pp. 55-58
    • Fritsches, K.A.1    Brill, R.W.2    Warrant, E.J.3
  • 39
    • 0025072784 scopus 로고
    • A possible new mechanism of oxygen affinity modulation in mammalian hemoglobins
    • Fronticelli, C. 1990. A possible new mechanism of oxygen affinity modulation in mammalian hemoglobins. Biophys Chem 37, 141-146.
    • (1990) Biophys Chem , vol.37 , pp. 141-146
    • Fronticelli, C.1
  • 42
    • 27744454384 scopus 로고    scopus 로고
    • Determination of P50 for feline hemoglobin
    • Herrmann, K. & Haskins, S. 2005. Determination of P50 for feline hemoglobin. J Vet Emerg Crit Care 15, 26-31.
    • (2005) J Vet Emerg Crit Care , vol.15 , pp. 26-31
    • Herrmann, K.1    Haskins, S.2
  • 43
    • 0022615764 scopus 로고
    • Die Primärstruktur der Hämoglobine von Eisbär (Ursus maritimus, Carnivora) and Kragenbär (Ursus tibetanus, Carnivora)
    • Hofmann, O., Schreitmuller, T. & Braunitzer, G. 1986. Die Primärstruktur der Hämoglobine von Eisbär (Ursus maritimus, Carnivora) and Kragenbär (Ursus tibetanus, Carnivora). Biol Chem Hoppe Seyler 367, 53-59.
    • (1986) Biol Chem Hoppe Seyler , vol.367 , pp. 53-59
    • Hofmann, O.1    Schreitmuller, T.2    Braunitzer, G.3
  • 44
    • 0021104746 scopus 로고
    • Oxygen equilibrium studies on hemoglobin from the bluefin tuna (Thunnus thynnus)
    • Ikeda-Saito, M., Yonetani, T. & Gibson, Q.H. 1983. Oxygen equilibrium studies on hemoglobin from the bluefin tuna (Thunnus thynnus). J Mol Biol 168, 673-686.
    • (1983) J Mol Biol , vol.168 , pp. 673-686
    • Ikeda-Saito, M.1    Yonetani, T.2    Gibson, Q.H.3
  • 45
    • 0030478168 scopus 로고    scopus 로고
    • Amino acid sequences of hemoglobin b chains of five species of pinnipeds: Neophoca cinerea, Otaria byronia, Eumetopias jubatus, Pusa hispida, and Pagophilus groenlandica
    • Ikehara, T., Eguchi, Y., Kayo, S. & Takei, H. 1996. Amino acid sequences of hemoglobin b chains of five species of pinnipeds: Neophoca cinerea, Otaria byronia, Eumetopias jubatus, Pusa hispida, and Pagophilus groenlandica. J Protein Chem 15, 659-665.
    • (1996) J Protein Chem , vol.15 , pp. 659-665
    • Ikehara, T.1    Eguchi, Y.2    Kayo, S.3    Takei, H.4
  • 46
    • 0005959019 scopus 로고
    • Physiological insulation of swine as bareskinned mammals
    • Irving, L. 1956. Physiological insulation of swine as bareskinned mammals. J Appl Physiol 9, 414-420.
    • (1956) J Appl Physiol , vol.9 , pp. 414-420
    • Irving, L.1
  • 47
    • 0000893704 scopus 로고
    • Temperature of skin in the arctic as a regulator of heat
    • Irving, L. & Krog, J. 1955. Temperature of skin in the arctic as a regulator of heat. J Appl Physiol 7, 355-364.
    • (1955) J Appl Physiol , vol.7 , pp. 355-364
    • Irving, L.1    Krog, J.2
  • 48
    • 0022704194 scopus 로고
    • Pronounced influence of Hb-O2 saturation on red cell pH in tench blood in vivo and in vitro
    • Jensen, F.B. 1986. Pronounced influence of Hb-O2 saturation on red cell pH in tench blood in vivo and in vitro. J Exp Zool 238, 119-124.
    • (1986) J Exp Zool , vol.238 , pp. 119-124
    • Jensen, F.B.1
  • 49
    • 0034967869 scopus 로고    scopus 로고
    • Hydrogen ion binding properties of tuna haemoglobins
    • Jensen, F.B. 2001. Hydrogen ion binding properties of tuna haemoglobins. Comp Biochem Physiol A Mol Integr Physiol 129, 511-517.
    • (2001) Comp Biochem Physiol A Mol Integr Physiol , vol.129 , pp. 511-517
    • Jensen, F.B.1
  • 50
    • 0023077250 scopus 로고
    • Thermodynamic analysis of precisely measured oxygen equilibria of tench hemoglobin and their dependence on ATP and protons
    • Jensen, F.B. & Weber, R.E. 1987. Thermodynamic analysis of precisely measured oxygen equilibria of tench hemoglobin and their dependence on ATP and protons. J Comp Physiol 157B, 137-143.
    • (1987) J Comp Physiol , vol.157 B , pp. 137-143
    • Jensen, F.B.1    Weber, R.E.2
  • 51
    • 0022002715 scopus 로고
    • Seasonal changes in the relative importance of different avenues of heat loss in resting and running reindeer
    • Johnsen, H.K., Rognmo, A., Nilssen, K.J. & Blix, A.S. 1985. Seasonal changes in the relative importance of different avenues of heat loss in resting and running reindeer. Acta Physiol Scand 123, 73-79.
    • (1985) Acta Physiol Scand , vol.123 , pp. 73-79
    • Johnsen, H.K.1    Rognmo, A.2    Nilssen, K.J.3    Blix, A.S.4
  • 52
    • 34250258336 scopus 로고
    • Aerobic and anaerobic metabolism during voluntary diving in Weddell seals - evidence of preferred pathways from blood-chemistry and behavior
    • Kooyman, G.L., Wahrenbrock, E.A., Castellini, M.A., Davis, R.W. & Sinnett, E.E. 1980. Aerobic and anaerobic metabolism during voluntary diving in Weddell seals - evidence of preferred pathways from blood-chemistry and behavior. J Comp Physiol 138, 335-346.
    • (1980) J Comp Physiol , vol.138 , pp. 335-346
    • Kooyman, G.L.1    Wahrenbrock, E.A.2    Castellini, M.A.3    Davis, R.W.4    Sinnett, E.E.5
  • 53
    • 84914496338 scopus 로고
    • The respiratory function of the blood in fishes
    • Krogh, A. & Leitch, I. 1919. The respiratory function of the blood in fishes. J Physiol (Lond) 52, 288-300.
    • (1919) J Physiol (Lond) , vol.52 , pp. 288-300
    • Krogh, A.1    Leitch, I.2
  • 55
    • 77951568885 scopus 로고    scopus 로고
    • Reversed temperature effect of haemoglobin oxygen binding in the porbeagle shark: potential implications for oxygen loss in the heat exchanger
    • Larsen, C. & Malte, H. 2003. Reversed temperature effect of haemoglobin oxygen binding in the porbeagle shark: potential implications for oxygen loss in the heat exchanger. Comp Biochem Physiol 134A, S18.
    • (2003) Comp Biochem Physiol , vol.134 A , pp. S18
    • Larsen, C.1    Malte, H.2
  • 56
    • 0042232406 scopus 로고    scopus 로고
    • ATP induced reverse temperature effect in iso-hemoglobins from the endothermic porbeagle shark (Lamna nasus)
    • Larsen, C., Malte, H. & Weber, R.E. 2003. ATP induced reverse temperature effect in iso-hemoglobins from the endothermic porbeagle shark (Lamna nasus). J Biol Chem 278, 30741-30747.
    • (2003) J Biol Chem , vol.278 , pp. 30741-30747
    • Larsen, C.1    Malte, H.2    Weber, R.E.3
  • 58
    • 8744291980 scopus 로고    scopus 로고
    • The pattern and process of mammoth evolution in Eurasia
    • Lister, A.M., Sher, A.V., van Essen, H. & Wei, G.B. 2005. The pattern and process of mammoth evolution in Eurasia. Quat Int 126-28, 49-64.
    • (2005) Quat Int , vol.126-128 , pp. 49-64
    • Lister, A.M.1    Sher, A.V.2    van Essen, H.3    Wei, G.B.4
  • 59
    • 0032143684 scopus 로고    scopus 로고
    • Responses of the red blood cells from two high-energy-demand teleosts, yellowfin tuna (Thunnus albacares) and skipjack tuna (Katsuwonus pelamis), to catecholamines
    • Lowe, T.E., Brill, R.W. & Cousins, K.L. 1998. Responses of the red blood cells from two high-energy-demand teleosts, yellowfin tuna (Thunnus albacares) and skipjack tuna (Katsuwonus pelamis), to catecholamines. J Comp Physiol B Biochem Syst Environ Physiol 168, 405-418.
    • (1998) J Comp Physiol B Biochem Syst Environ Physiol , vol.168 , pp. 405-418
    • Lowe, T.E.1    Brill, R.W.2    Cousins, K.L.3
  • 60
    • 0000358901 scopus 로고    scopus 로고
    • Blood oxygenbinding characteristics of big-eye tuna (Thunnus obesus), a high-energy-demand teleost that is tolerant of low ambient oxygen
    • Lowe, T.E., Brill, R.W. & Cousins, K.L. 2000. Blood oxygenbinding characteristics of big-eye tuna (Thunnus obesus), a high-energy-demand teleost that is tolerant of low ambient oxygen. Mar Biol 136, 1087-1098.
    • (2000) Mar Biol , vol.136 , pp. 1087-1098
    • Lowe, T.E.1    Brill, R.W.2    Cousins, K.L.3
  • 61
    • 1842483305 scopus 로고    scopus 로고
    • The structure-function relationship of hemoglobin in solution at atomic resolution
    • Lukin, J.A. & Ho, C. 2004. The structure-function relationship of hemoglobin in solution at atomic resolution. Chem Rev 104, 1219-1230.
    • (2004) Chem Rev , vol.104 , pp. 1219-1230
    • Lukin, J.A.1    Ho, C.2
  • 63
    • 67649308436 scopus 로고    scopus 로고
    • Origin and ascendancy of a chimeric fusion gene: the b/d-globin gene of paenungulate mammals
    • Opazo, J.C., Sloan, A.M., Campbell, K.L. & Storz, J.F. 2009. Origin and ascendancy of a chimeric fusion gene: the b/d-globin gene of paenungulate mammals. Mol Biol Evol 26, 1469-1478.
    • (2009) Mol Biol Evol , vol.26 , pp. 1469-1478
    • Opazo, J.C.1    Sloan, A.M.2    Campbell, K.L.3    Storz, J.F.4
  • 64
    • 0842286524 scopus 로고
    • Temperature regulation of the polar bear (Thalarctos maritimus)
    • Øritsland, N.A. 1970. Temperature regulation of the polar bear (Thalarctos maritimus). Comp Biochem Physiol 37, 225-233.
    • (1970) Comp Biochem Physiol , vol.37 , pp. 225-233
    • Øritsland, N.A.1
  • 65
    • 0021004799 scopus 로고
    • Species adaptation in a protein molecule
    • Perutz, M.F. 1983. Species adaptation in a protein molecule. Mol Biol Evol 1, 1-28.
    • (1983) Mol Biol Evol , vol.1 , pp. 1-28
    • Perutz, M.F.1
  • 66
    • 0018860147 scopus 로고
    • Regulation of oxygen affinity of mammalian haemoglobins
    • Perutz, M.F. & 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
  • 69
    • 0019420982 scopus 로고
    • Oxygen equilibrium properties of blood and hemoglobin of fetal and adult Weddell seals
    • Qvist, J., Weber, R.E. & Zapol, W.M. 1981. Oxygen equilibrium properties of blood and hemoglobin of fetal and adult Weddell seals. J Appl Physiol 50, 999-1005.
    • (1981) J Appl Physiol , vol.50 , pp. 999-1005
    • Qvist, J.1    Weber, R.E.2    Zapol, W.M.3
  • 70
    • 0001502640 scopus 로고
    • Distribution of acid-soluble phosphorus in the blood cells of various vertebrates
    • Rapoport, S. & Guest, G.M. 1941. Distribution of acid-soluble phosphorus in the blood cells of various vertebrates. J Biol Chem 138, 269-282.
    • (1941) J Biol Chem , vol.138 , pp. 269-282
    • Rapoport, S.1    Guest, G.M.2
  • 71
    • 0025083377 scopus 로고
    • Effect of temperature on oxygen affinity and anion binding of bovine hemoglobin
    • Razynska, A., Fronticelli, C., Di Cera, E., Gryczynski, Z. & Bucci, E. 1990. Effect of temperature on oxygen affinity and anion binding of bovine hemoglobin. Biophys Chem 38, 111-115.
    • (1990) Biophys Chem , vol.38 , pp. 111-115
    • Razynska, A.1    Fronticelli, C.2    Di Cera, E.3    Gryczynski, Z.4    Bucci, E.5
  • 72
    • 0023836405 scopus 로고
    • The Bohr effect
    • Riggs, A.F. 1988. The Bohr effect. Annu Rev Physiol 50, 181-204.
    • (1988) Annu Rev Physiol , vol.50 , pp. 181-204
    • Riggs, A.F.1
  • 73
    • 33644524361 scopus 로고    scopus 로고
    • A globin in every cell?
    • Riggs, A.F. & Gorr, T.A. 2006. A globin in every cell? PNAS 103, 2469-2470.
    • (2006) PNAS , vol.103 , pp. 2469-2470
    • Riggs, A.F.1    Gorr, T.A.2
  • 74
    • 34548223646 scopus 로고    scopus 로고
    • Proboscidean mitogenomics: chronology and mode of elephant evolution using mastodon as outgroup
    • Rohland, N., Malaspinas, A.S., Pollack, J.L., Slatkin, M., Matheus, P. & Hofreiter, M. 2007. Proboscidean mitogenomics: chronology and mode of elephant evolution using mastodon as outgroup. PLoS Biol 5, 1663-1671.
    • (2007) PLoS Biol , vol.5 , pp. 1663-1671
    • Rohland, N.1    Malaspinas, A.S.2    Pollack, J.L.3    Slatkin, M.4    Matheus, P.5    Hofreiter, M.6
  • 75
    • 36949090402 scopus 로고
    • Oxygen equilibrium of haemoglobin from Thunnus thynnus
    • Rossi-Fanelli, A., Antonini, E. & Giuffrè, R. 1960. Oxygen equilibrium of haemoglobin from Thunnus thynnus. Nature 186, 895-897.
    • (1960) Nature , vol.186 , pp. 895-897
    • Rossi-Fanelli, A.1    Antonini, E.2    Giuffrè, R.3
  • 76
    • 58149165358 scopus 로고    scopus 로고
    • Hemoglobin research and the origins of molecular medicine
    • Schechter, A.N. 2008. Hemoglobin research and the origins of molecular medicine. Blood 112, 3927-3938.
    • (2008) Blood , vol.112 , pp. 3927-3938
    • Schechter, A.N.1
  • 77
    • 0001596450 scopus 로고
    • Counter-current vascular heat exchange in the fins of whales
    • Scholander, P.F. & Schevill, W.E. 1955. Counter-current vascular heat exchange in the fins of whales. J Appl Physiol 8, 279-282.
    • (1955) J Appl Physiol , vol.8 , pp. 279-282
    • Scholander, P.F.1    Schevill, W.E.2
  • 78
    • 0017048031 scopus 로고
    • Functional aspects of hemoglobin evolution in the mammals
    • Scott, A.F., Bunn, H.F. & Brush, A.H. 1976. Functional aspects of hemoglobin evolution in the mammals. J Mol Evol 8, 311-316.
    • (1976) J Mol Evol , vol.8 , pp. 311-316
    • Scott, A.F.1    Bunn, H.F.2    Brush, A.H.3
  • 79
    • 0017519961 scopus 로고
    • The phylogenetic distribution of red cell 2,3 diphosphoglycerate and its interaction with mammalian hemoglobins
    • Scott, A.F., Bunn, H.F. & Brush, A.H. 1977. The phylogenetic distribution of red cell 2,3 diphosphoglycerate and its interaction with mammalian hemoglobins. J Exp Zool 201, 269-288.
    • (1977) J Exp Zool , vol.201 , pp. 269-288
    • Scott, A.F.1    Bunn, H.F.2    Brush, A.H.3
  • 80
    • 17244377098 scopus 로고    scopus 로고
    • Temperature alters the respiratory surface area of crucian carp Carassius carassius and goldfish Carassius auratus
    • Sollid, J., Weber, R.E. & Nilsson, G.E. 2005. Temperature alters the respiratory surface area of crucian carp Carassius carassius and goldfish Carassius auratus. J Exp Biol 208, 1109-1116.
    • (2005) J Exp Biol , vol.208 , pp. 1109-1116
    • Sollid, J.1    Weber, R.E.2    Nilsson, G.E.3
  • 81
    • 0016268318 scopus 로고
    • Organic phosphates and hemoglobin structure-function relationships in the feline
    • Taketa, F. 1974. Organic phosphates and hemoglobin structure-function relationships in the feline. Ann N Y Acad Sci 241, 524-537.
    • (1974) Ann N Y Acad Sci , vol.241 , pp. 524-537
    • Taketa, F.1
  • 82
    • 0028284553 scopus 로고
    • Adaptation to extreme environments: structure-function relationships in Emperor penguin haemoglobin
    • Tamburrini, M., Condo, S.G., di, P.G. & Giardina, B. 1994. Adaptation to extreme environments: structure-function relationships in Emperor penguin haemoglobin. J Mol Biol 237, 615-621.
    • (1994) J Mol Biol , vol.237 , pp. 615-621
    • Tamburrini, M.1    Condo, S.G.2    di, P.G.3    Giardina, B.4
  • 83
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: functions and molecular adaptations
    • Weber, R.E. & Vinogradov, S.N. 2001. Nonvertebrate hemoglobins: functions and molecular adaptations. Physiol Rev 81, 569-628.
    • (2001) Physiol Rev , vol.81 , pp. 569-628
    • Weber, R.E.1    Vinogradov, S.N.2
  • 84
    • 0000602219 scopus 로고
    • S.C. Wood (ed.) Lung Biology in Health and Disease. Comparative Pulmonary Physiology, Current Concepts, Marcel Dekker, Inc., New York.
    • Weber, R.E. & Wells, R.M.G. (1989) Hemoglobin structure and function. In: S.C. Wood (ed.) Lung Biology in Health and Disease. Comparative Pulmonary Physiology, Current Concepts, pp. 279-310. Marcel Dekker, Inc., New York.
    • (1989) Hemoglobin structure and function , pp. 279-310
    • Weber, R.E.1    Wells, R.M.G.2
  • 86
    • 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
    • Weber, R.E., Jensen, F.B.& Cox, R.P. 1987a. 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, 145-152.
    • (1987) J Comp Physiol , vol.157 B , pp. 145-152
    • Weber, R.E.1    Jensen, F.B.2    Cox, R.P.3
  • 87
    • 0023247381 scopus 로고
    • Embryonic pig hemoglobins Gower I (ν2ε2), Gower II (α2ε2),Heide I (ζ2ν2) and Heide II (α2ν2): oxygen-binding functions related to structure and embryonic oxygen supply
    • Weber, R.E., Kleinschmidt, T. & Braunitzer, G. 1987b. Embryonic pig hemoglobins Gower I (ν2ε2), Gower II (α2ε2),Heide I (ζ2ν2) and Heide II (α2ν2): oxygen-binding functions related to structure and embryonic oxygen supply. Respir Physiol 69, 347-357.
    • (1987) Respir Physiol , vol.69 , pp. 347-357
    • Weber, R.E.1    Kleinschmidt, T.2    Braunitzer, G.3
  • 88
    • 0042928294 scopus 로고    scopus 로고
    • Hemoglobin function in deep-sea and hydrothermal-vent endemic fish: Symenchelis parasitica (Anguillidae) and Thermarces cerberus (Zoarcidae)
    • Weber, R.E., Hourdez, S., Knowles, F. & Lallier, F. 2003. Hemoglobin function in deep-sea and hydrothermal-vent endemic fish: Symenchelis parasitica (Anguillidae) and Thermarces cerberus (Zoarcidae). J Exp Biol 206, 2693.
    • (2003) J Exp Biol , vol.206 , pp. 2693
    • Weber, R.E.1    Hourdez, S.2    Knowles, F.3    Lallier, F.4
  • 89
    • 43049145521 scopus 로고    scopus 로고
    • Thermodynamics of oxygenation-linked proton and lactate binding govern the temperature sensitivity O2 binding in crustacean (Carcinus maenas) haemocyanin
    • Weber, R.E., Behrens, J.W., Malte, H. & Fago, A. 2008. Thermodynamics of oxygenation-linked proton and lactate binding govern the temperature sensitivity O2 binding in crustacean (Carcinus maenas) haemocyanin. J Exp Biol 211, 1057-1062.
    • (2008) J Exp Biol , vol.211 , pp. 1057-1062
    • Weber, R.E.1    Behrens, J.W.2    Malte, H.3    Fago, A.4
  • 90
    • 77951588546 scopus 로고    scopus 로고
    • ATP-induced temperature independence of hemoglobin-O2 affinity in heterothermic billfish
    • Weber, R.E., Campbell, K.L., Fago, A., Malte, H. & Jensen, F.B. 2010. ATP-induced temperature independence of hemoglobin-O2 affinity in heterothermic billfish. J Exp Biol 213, 1579-1585.
    • (2010) J Exp Biol , vol.213 , pp. 1579-1585
    • Weber, R.E.1    Campbell, K.L.2    Fago, A.3    Malte, H.4    Jensen, F.B.5
  • 91
    • 0018413150 scopus 로고
    • Oxygen equilibrium properties of isolated haemoglobins from the weddell seal Leptonychotes weddelli
    • Wells, R.M. & Brennan, S.O. 1979. Oxygen equilibrium properties of isolated haemoglobins from the weddell seal Leptonychotes weddelli. Comp Biochem Physiol A Mol Integr Physiol 63, 365-368.
    • (1979) Comp Biochem Physiol A Mol Integr Physiol , vol.63 , pp. 365-368
    • Wells, R.M.1    Brennan, S.O.2
  • 92
    • 0022616633 scopus 로고
    • Modest effect of temperature on the porcine oxygen dissociation curve
    • Willford, D.C. & Hill, E.P. 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
  • 93
    • 0025101258 scopus 로고
    • Temperature and the oxygen-hemoglobin dissociation curve of the harbor seal, Phoca vitulina
    • Willford, D.C., Gray, A.T., Hempleman, S.C., Davis, R.W. & Hill, E.P. 1990. Temperature and the oxygen-hemoglobin dissociation curve of the harbor seal, Phoca vitulina. Respir Physiol 79, 137-144.
    • (1990) Respir Physiol , vol.79 , pp. 137-144
    • Willford, D.C.1    Gray, A.T.2    Hempleman, S.C.3    Davis, R.W.4    Hill, E.P.5
  • 94
    • 0017875962 scopus 로고
    • Temperature acclimation in the pancake tortoise, Malacochersus tornieri: metabolic rate, blood pH, oxygen affinity and red cell organic phosphates
    • Wood, S.C., Lykkeboe, G., Johansen, K., Weber, R.E. & Maloiy, G.M.O. 1978. Temperature acclimation in the pancake tortoise, Malacochersus tornieri: metabolic rate, blood pH, oxygen affinity and red cell organic phosphates. Comp Biochem Physiol 59A, 155-160.
    • (1978) Comp Biochem Physiol , vol.59 A , pp. 155-160
    • Wood, S.C.1    Lykkeboe, G.2    Johansen, K.3    Weber, R.E.4    Maloiy, G.M.O.5
  • 95
    • 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. Adv Protein Chem 19, 223-286.
    • (1964) Adv Protein Chem , vol.19 , pp. 223-286
    • Wyman, J.1


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