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Volumn 27, Issue C, 2009, Pages 255-299

Chapter 6 Blood‐Gas Transport and Hemoglobin Function: Adaptations for Functional and Environmental Hypoxia

(1)  Wells, Rufus M G a  

a NONE

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EID: 84998950149     PISSN: 15465098     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1546-5098(08)00006-X     Document Type: Chapter
Times cited : (98)

References (205)
  • 1
    • 0022135689 scopus 로고
    • Role of histidine‐related compounds to intracellular buffering in fish skeletal muscle
    • H. Abe G.P. Dobson U. Hoeger W.S. Parkhouse Role of histidine‐related compounds to intracellular buffering in fish skeletal muscle Am. J. Physiol. 249 1985 R449 R454
    • (1985) Am. J. Physiol. , vol.249 , pp. R449-R454
    • Abe, H.1    Dobson, G.P.2    Hoeger, U.3    Parkhouse, W.S.4
  • 3
    • 0020528854 scopus 로고
    • Effect of acclimation temperature on oxygen transport in the blood of the carp, Cyprinus carpio
    • C. Albers R. Manz D. Muster G.M. Hughes Effect of acclimation temperature on oxygen transport in the blood of the carp, Cyprinus carpio Resp. Physiol. 52 1983 165 179
    • (1983) Resp. Physiol. , vol.52 , pp. 165-179
    • Albers, C.1    Manz, R.2    Muster, D.3    Hughes, G.M.4
  • 4
    • 0031259561 scopus 로고    scopus 로고
    • Why do tuna maintain elevated slow muscle temperatures? Power output of muscle isolated from endothermic and ectothermic fish
    • J.D. Altringham B.A. Block Why do tuna maintain elevated slow muscle temperatures? Power output of muscle isolated from endothermic and ectothermic fish J. Exp. Biol. 200 1997 2617 2627
    • (1997) J. Exp. Biol. , vol.200 , pp. 2617-2627
    • Altringham, J.D.1    Block, B.A.2
  • 5
    • 33749080771 scopus 로고    scopus 로고
    • Cardiac expression and distribution of nitric oxide synthases in the ventricle of the cold‐adapted Antarctic teleosts, the hemoglobinless Chionodraca hamatus and the red‐blooded Trematomus bernacchii
    • D. Amelio F. Garofalo D. Pellegrino F. Giordano B. Tota M.C. Cerra Cardiac expression and distribution of nitric oxide synthases in the ventricle of the cold‐adapted Antarctic teleosts, the hemoglobinless Chionodraca hamatus and the red‐blooded Trematomus bernacchii Nitric Oxide 15 2006 190 198
    • (2006) Nitric Oxide , vol.15 , pp. 190-198
    • Amelio, D.1    Garofalo, F.2    Pellegrino, D.3    Giordano, F.4    Tota, B.5    Cerra, M.C.6
  • 6
    • 0021944642 scopus 로고
    • Seasonal variations in hematocrit, red cell hemoglobin and nucleoside triphosphate concentrations, in the European eel Anguilla anguilla
    • N.A. Andersen J.S. Laursen G. Lykkeboe Seasonal variations in hematocrit, red cell hemoglobin and nucleoside triphosphate concentrations, in the European eel Anguilla anguilla Comp. Biochem. Physiol. 81A 1985 87 92
    • (1985) Comp. Biochem. Physiol. , vol.81A , pp. 87-92
    • Andersen, N.A.1    Laursen, J.S.2    Lykkeboe, G.3
  • 7
    • 0023007873 scopus 로고
    • Function of myoglobin in oxygen consumption by isolated perfused fish hearts
    • J.R. Bailey W.R. Driedzic Function of myoglobin in oxygen consumption by isolated perfused fish hearts Am. J. Physiol. Regul. Itegr. Comp. Physiol. 251 1986 R1144 R1150
    • (1986) Am. J. Physiol. Regul. Itegr. Comp. Physiol. , vol.251 , pp. R1144-R1150
    • Bailey, J.R.1    Driedzic, W.R.2
  • 8
    • 27744570752 scopus 로고    scopus 로고
    • Juvenile Atlantic and shortnose sturgeons (Family: Acipenseridae) have different hematological responses to acute environmental hypoxia
    • D.W. Baker A.M. Wood J.D. Kieffer Juvenile Atlantic and shortnose sturgeons (Family: Acipenseridae) have different hematological responses to acute environmental hypoxia Physiol. Biochem. Zool. 78 2005 916 925
    • (2005) Physiol. Biochem. Zool. , vol.78 , pp. 916-925
    • Baker, D.W.1    Wood, A.M.2    Kieffer, J.D.3
  • 9
    • 28144442070 scopus 로고
    • Oxygen transport potential in tropical elasmobranchs from the Great Barrier Reef: Relationship between haematology and blood viscosity
    • J. Baldwin R.M.G. Wells Oxygen transport potential in tropical elasmobranchs from the Great Barrier Reef: Relationship between haematology and blood viscosity J. Exp. Mar. Biol. Ecol. 144 1990 145 155
    • (1990) J. Exp. Mar. Biol. Ecol. , vol.144 , pp. 145-155
    • Baldwin, J.1    Wells, R.M.G.2
  • 11
    • 0343527323 scopus 로고    scopus 로고
    • O2‐dependent K+ fluxes in trout red blood cells: The nature of O2 sensing revealed by the O2 affinity, cooperativity and pH dependence of transport
    • 2 affinity, cooperativity and pH dependence of transport J. Physiol. 526 2000 69 80
    • (2000) J. Physiol. , vol.526 , pp. 69-80
    • Berenbrink, M.1    Völkel, S.2    Heisler, N.3    Nikinmaa, M.4
  • 12
    • 15244349241 scopus 로고    scopus 로고
    • Evolution of oxygen secretion in fishes and the emergence of a complex physiological system
    • M. Berenbrink P. Koldkjær O. Kepp A.R. Cousins Evolution of oxygen secretion in fishes and the emergence of a complex physiological system Science 307 2005 1752 1757
    • (2005) Science , vol.307 , pp. 1752-1757
    • Berenbrink, M.1    Koldkjær, P.2    Kepp, O.3    Cousins, A.R.4
  • 13
    • 33750818912 scopus 로고    scopus 로고
    • GEOCARBSULF: A combined model for Phanaerozoic atmospheric O2 and CO2
    • 2 Geochim. Cosmochim. Ac. 70 2006 5653 5664
    • (2006) Geochim. Cosmochim. Ac. , vol.70 , pp. 5653-5664
    • Berner, R.A.1
  • 15
    • 85120198222 scopus 로고
    • Regulation of brain and eye temperatures of the bluefin tuna
    • B.A. Block F.G. Carey Regulation of brain and eye temperatures of the bluefin tuna Comp. Biochem. Physiol. 43A 1985 425 433
    • (1985) Comp. Biochem. Physiol. , vol.43A , pp. 425-433
    • Block, B.A.1    Carey, F.G.2
  • 17
    • 7944224443 scopus 로고    scopus 로고
    • New insights into the proton‐dependent oxygen affinity of Root effect haemoglobins
    • C. Bonaventura A.L. Crumbliss R.E. Weber New insights into the proton‐dependent oxygen affinity of Root effect haemoglobins Acta Physiol. Scand. 182 2004 245 258
    • (2004) Acta Physiol. Scand. , vol.182 , pp. 245-258
    • Bonaventura, C.1    Crumbliss, A.L.2    Weber, R.E.3
  • 18
    • 0023628877 scopus 로고
    • Acute exposure to graded levels of hypoxia in rainbow trout (Salmo gairdneri): Metabolic and respiratory adaptations
    • R.G. Boutilier G. Dobson U. Hoeger D.J. Randall Acute exposure to graded levels of hypoxia in rainbow trout ( Salmo gairdneri ): Metabolic and respiratory adaptations Resp. Physiol. 71 1988 69 82
    • (1988) Resp. Physiol. , vol.71 , pp. 69-82
    • Boutilier, R.G.1    Dobson, G.2    Hoeger, U.3    Randall, D.J.4
  • 19
    • 33745982132 scopus 로고    scopus 로고
    • The optimal oxygen equilibrium curve: A comparison between environmental hypoxia and anaemia
    • C.J. Brauner T. Wang The optimal oxygen equilibrium curve: A comparison between environmental hypoxia and anaemia Amer. Zool. 37 1997 101 108
    • (1997) Amer. Zool. , vol.37 , pp. 101-108
    • Brauner, C.J.1    Wang, T.2
  • 20
    • 0032168138 scopus 로고    scopus 로고
    • Hydrogen ion titrations of the anodic and cathodic haemoglobin components of the European eel Anguilla anguilla
    • C.J. Brauner R.E. Weber Hydrogen ion titrations of the anodic and cathodic haemoglobin components of the European eel Anguilla anguilla J. Exp. Biol. 201 1998 2507 2514
    • (1998) J. Exp. Biol. , vol.201 , pp. 2507-2514
    • Brauner, C.J.1    Weber, R.E.2
  • 21
    • 85120190757 scopus 로고    scopus 로고
    • Oxygen transfer
    • C.J. Brauner A.L. Val Oxygen transfer A.L. Val V.M.F. de Almeida‐Val D.J. Randall The Physiology of Tropical Fishes W.S. Hoar D.J. Randall A.P. Farrell Fish Physiology Vol. 21 2006 Academic Press London 277 306
    • (2006) , pp. 277-306
    • Brauner, C.J.1    Val, A.L.2
  • 22
    • 33750973397 scopus 로고    scopus 로고
    • Effects of open‐ and closed‐system temperature changes on blood O2‐binding characteristics of Atlantic bluefin tuna (Thunnus thynnus)
    • 2‐binding characteristics of Atlantic bluefin tuna ( Thunnus thynnus ) Fish Physiol. Biochem. 32 2006 283 294
    • (2006) Fish Physiol. Biochem. , vol.32 , pp. 283-294
    • Brill, R.W.1    Bushnell, P.G.2
  • 23
    • 37549056580 scopus 로고    scopus 로고
    • Effects of anaerobic exercise accompanying catch‐and‐release fishing on blood‐oxygen affinity of the sandbar shark (Carcharhinus plumbeus, Nardo)
    • R. Brill P. Bushnell S. Schroff M. Seifert M. Galvin Effects of anaerobic exercise accompanying catch‐and‐release fishing on blood‐oxygen affinity of the sandbar shark ( Carcharhinus plumbeus , Nardo) J. Exp. Mar. Biol. Ecol. 354 2008 132 143
    • (2008) J. Exp. Mar. Biol. Ecol. , vol.354 , pp. 132-143
    • Brill, R.1    Bushnell, P.2    Schroff, S.3    Seifert, M.4    Galvin, M.5
  • 24
    • 10444228083 scopus 로고    scopus 로고
    • Root effect hemoglobins
    • T. Brittain Root effect hemoglobins J. Inorg. Biochem. 99 2005 120 129
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 120-129
    • Brittain, T.1
  • 25
    • 44749091800 scopus 로고    scopus 로고
    • Extreme pH sensitivity in the binding of oxygen to some fish hemoglobins in the Root effect
    • T. Brittain Extreme pH sensitivity in the binding of oxygen to some fish hemoglobins in the Root effect A Ghosh The Smallest Biomolecules. Diatomics and their Interactions with Heme Proteins 2008 Elsevier UK 219 234
    • (2008) , pp. 219-234
    • Brittain, T.1
  • 26
    • 0031699342 scopus 로고    scopus 로고
    • An ecophysiological interpretation of hemoglobin multiplicity in three herbivorous marine teleost species from New Zealand
    • O. Brix K.D. Clements R.M.G. Wells An ecophysiological interpretation of hemoglobin multiplicity in three herbivorous marine teleost species from New Zealand Comp. Biochem. Physiol. 121A 1998 189 195
    • (1998) Comp. Biochem. Physiol. , vol.121A , pp. 189-195
    • Brix, O.1    Clements, K.D.2    Wells, R.M.G.3
  • 27
    • 0032007132 scopus 로고    scopus 로고
    • Genetic variation and functional properties of Atlantic cod haemoglobins: Introducing a modified tonometric method for studying fragile haemoglobins
    • O. Brix E. Forås I. Strand Genetic variation and functional properties of Atlantic cod haemoglobins: Introducing a modified tonometric method for studying fragile haemoglobins Comp. Biochem. Physiol. 119A 1998 575 583
    • (1998) Comp. Biochem. Physiol. , vol.119A , pp. 575-583
    • Brix, O.1    Forås, E.2    Strand, I.3
  • 28
    • 0032770545 scopus 로고    scopus 로고
    • Haemoglobin components and oxygen transport in relation to habitat distribution in triplefin fishes (Tripterygiidae)
    • O. Brix K.D. Clements R.M.G. Wells Haemoglobin components and oxygen transport in relation to habitat distribution in triplefin fishes (Tripterygiidae) J. Comp. Physiol. 169B 1999 329 334
    • (1999) J. Comp. Physiol. , vol.169B , pp. 329-334
    • Brix, O.1    Clements, K.D.2    Wells, R.M.G.3
  • 30
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: A novel globin type ubiquitously expressed in vertebrate tissues
    • T. Burmester B. Ebner B. Weich 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
  • 31
    • 33646593142 scopus 로고    scopus 로고
    • Blood sampling techniques and storage duration: Effects on the presence and magnitude of the red blood cell β‐adrenergic response in rainbow trout (Oncorhynchus mykiss)
    • S. Caldwell J.L. Rummer C.J. Brauner Blood sampling techniques and storage duration: Effects on the presence and magnitude of the red blood cell β‐adrenergic response in rainbow trout ( Oncorhynchus mykiss ) Comp. Biochem. Physiol. 144A 2006 188 195
    • (2006) Comp. Biochem. Physiol. , vol.144A , pp. 188-195
    • Caldwell, S.1    Rummer, J.L.2    Brauner, C.J.3
  • 33
    • 0023160622 scopus 로고
    • Evidence that myoglobin does not support heart performance at maximal levels of oxygen demand
    • A.A. Canty W.R. Driedzic Evidence that myoglobin does not support heart performance at maximal levels of oxygen demand J. Exp. Biol. 128 1987 469 473
    • (1987) J. Exp. Biol. , vol.128 , pp. 469-473
    • Canty, A.A.1    Driedzic, W.R.2
  • 34
    • 33846544872 scopus 로고    scopus 로고
    • Improving sneaky‐sex in a low oxygen environment: Reproductive and physiological responses of male mosquito fish to chronic hypoxia
    • A.J. Carter R.S. Wilson Improving sneaky‐sex in a low oxygen environment: Reproductive and physiological responses of male mosquito fish to chronic hypoxia J. Exp. Biol. 209 2006 4878 4884
    • (2006) J. Exp. Biol. , vol.209 , pp. 4878-4884
    • Carter, A.J.1    Wilson, R.S.2
  • 35
    • 0004760138 scopus 로고
    • Temperature‐induced changes in blood gas equilibria in the albacore, Thunnus alalunga, a warm‐bodied tuna
    • J.J. Cech R.M. Laurs J.B. Graham Temperature‐induced changes in blood gas equilibria in the albacore, Thunnus alalunga , a warm‐bodied tuna J. Exp. Biol. 109 1984 21 34
    • (1984) J. Exp. Biol. , vol.109 , pp. 21-34
    • Cech, J.J.1    Laurs, R.M.2    Graham, J.B.3
  • 36
    • 0036848727 scopus 로고    scopus 로고
    • Physiological refugia: Hypoxia tolerance and maintenance of fish diversity in the Lake Victoria region
    • L.J. Chapman C.A. Chapman F.G. Nordlie A.E. Rosenberger Physiological refugia: Hypoxia tolerance and maintenance of fish diversity in the Lake Victoria region Comp. Biochem. Physiol. 133A 2002 421 437
    • (2002) Comp. Biochem. Physiol. , vol.133A , pp. 421-437
    • Chapman, L.J.1    Chapman, C.A.2    Nordlie, F.G.3    Rosenberger, A.E.4
  • 37
    • 38749146549 scopus 로고    scopus 로고
    • Devonian climate change, breathing, and the origin of the tetrapod stem group
    • J.A. Clack Devonian climate change, breathing, and the origin of the tetrapod stem group Integ. Comp. Biol. 47 2007 510 523
    • (2007) Integ. Comp. Biol. , vol.47 , pp. 510-523
    • Clack, J.A.1
  • 38
    • 44749085304 scopus 로고    scopus 로고
    • Thermal effects on the blood respiratory properties of southern bluefin tuna, Thunnus maccoyii
    • T.D. Clark R.S. Seymour R.M.G. Wells P.B. Frappell Thermal effects on the blood respiratory properties of southern bluefin tuna, Thunnus maccoyii Comp. Biochem. Physiol. 150A 2008 239 246
    • (2008) Comp. Biochem. Physiol. , vol.150A , pp. 239-246
    • Clark, T.D.1    Seymour, R.S.2    Wells, R.M.G.3    Frappell, P.B.4
  • 39
    • 0034532570 scopus 로고    scopus 로고
    • A cluster of four globin genes from the Antarctic fish Notothenia coriiceps
    • E. Cocca H.W. Detrich S.K. Parker G. di Prisco A cluster of four globin genes from the Antarctic fish Notothenia coriiceps J. Fish Biol. 57 Suppl. A 2000 33 50
    • (2000) J. Fish Biol. , vol.57 , Issue.Suppl. A , pp. 33-50
    • Cocca, E.1    Detrich, H.W.2    Parker, S.K.3    di Prisco, G.4
  • 40
    • 0031895009 scopus 로고    scopus 로고
    • Effects of hypercapnia on blood‐gas and acid‐base states in the white sturgeon, Acipenser transmontanus
    • C.E. Crocker J.J. Cech Effects of hypercapnia on blood‐gas and acid‐base states in the white sturgeon, Acipenser transmontanus J. Comp. Physiol. 198B 1998 50 60
    • (1998) J. Comp. Physiol. , vol.198B , pp. 50-60
    • Crocker, C.E.1    Cech, J.J.2
  • 41
    • 0031424957 scopus 로고    scopus 로고
    • The hemoglobin system of Antarctic and non‐Antarctic notothenioid fishes
    • R. D'Avino G. di Prisco The hemoglobin system of Antarctic and non‐Antarctic notothenioid fishes Comp. Biochem. Physiol. 118A 1997 1045 1049
    • (1997) Comp. Biochem. Physiol. , vol.118A , pp. 1045-1049
    • D'Avino, R.1    di Prisco, G.2
  • 42
    • 0030921939 scopus 로고    scopus 로고
    • Asymmetric hemoglobins, their thiol content, and blood glutathione of the scalloped hammerhead shark, Sphyrna lewini
    • A.L. Dafre E. Reischl Asymmetric hemoglobins, their thiol content, and blood glutathione of the scalloped hammerhead shark, Sphyrna lewini Comp. Biochem. Physiol. 116B 1997 323 331
    • (1997) Comp. Biochem. Physiol. , vol.116B , pp. 323-331
    • Dafre, A.L.1    Reischl, E.2
  • 43
    • 0032532693 scopus 로고    scopus 로고
    • Oxidative stress causes intracellular reversible S‐thiolation of chicken haemoglobin under diamide and xanthine oxidase treatment
    • A.L. Dafre E. Reischl Oxidative stress causes intracellular reversible S ‐thiolation of chicken haemoglobin under diamide and xanthine oxidase treatment Arch. Biochem. Biophys. 358 1998 291 296
    • (1998) Arch. Biochem. Biophys. , vol.358 , pp. 291-296
    • Dafre, A.L.1    Reischl, E.2
  • 44
    • 0022669961 scopus 로고
    • Effects of sustained swimming on rainbow trout muscle structure, blood oxygen transport, and lactate dehydrogenase isozymes: Evidence for increased aerobic capacity of white muscle
    • P.S. Davie R.M.G. Wells V. Tetens Effects of sustained swimming on rainbow trout muscle structure, blood oxygen transport, and lactate dehydrogenase isozymes: Evidence for increased aerobic capacity of white muscle J. Exp. Zool. 237 1986 159 171
    • (1986) J. Exp. Zool. , vol.237 , pp. 159-171
    • Davie, P.S.1    Wells, R.M.G.2    Tetens, V.3
  • 45
    • 38749093406 scopus 로고    scopus 로고
    • Negative cooperativity in Root effect hemoglobins: Role of heterogeneity
    • H. Deker H. Nadja Negative cooperativity in Root effect hemoglobins: Role of heterogeneity Integr. Comp. Biol. 47 2007 656 661
    • (2007) Integr. Comp. Biol. , vol.47 , pp. 656-661
    • Deker, H.1    Nadja, H.2
  • 47
    • 0001533207 scopus 로고
    • Partial characterization of the buffering components of the red and white myotomal muscle of marine teleosts, with special emphasis on scombrid fishes
    • K.A. Dickson G.N. Somero Partial characterization of the buffering components of the red and white myotomal muscle of marine teleosts, with special emphasis on scombrid fishes Physiol. Zool. 60 1987 699 706
    • (1987) Physiol. Zool. , vol.60 , pp. 699-706
    • Dickson, K.A.1    Somero, G.N.2
  • 48
    • 0026659611 scopus 로고
    • The hemoglobins of marine and freshwater fish: The search for correlations with physiological adaptation
    • G. di Prisco M. Tamburrini The hemoglobins of marine and freshwater fish: The search for correlations with physiological adaptation Comp. Biochem. Physiol. 102B 1992 661 671
    • (1992) Comp. Biochem. Physiol. , vol.102B , pp. 661-671
    • di Prisco, G.1    Tamburrini, M.2
  • 50
    • 0003380827 scopus 로고    scopus 로고
    • Oxygen transport systems in extreme environments: Multiplicity and structure‐function relationship in haemoglobins of Antarctic fish
    • G. di Prisco M. Tamburrini R. D'Avino Oxygen transport systems in extreme environments: Multiplicity and structure‐function relationship in haemoglobins of Antarctic fish H.O. Pörtner R.C. Playle Cold Ocean Physiology Society for Experimental Biology Series 66 1998 Cambridge University Press Cambridge 143 165
    • (1998) , pp. 143-165
    • di Prisco, G.1    Tamburrini, M.2    D'Avino, R.3
  • 51
    • 0029913169 scopus 로고    scopus 로고
    • Different mechanisms of glutathione‐protein mixed disulphides of diamide and tert‐butyl hydroperoxide in rat blood
    • P. Di Simplico E. Lupis R. Rossi Different mechanisms of glutathione‐protein mixed disulphides of diamide and tert ‐butyl hydroperoxide in rat blood Biochim. Biophys. Acta 1289 1996 252 260
    • (1996) Biochim. Biophys. Acta , vol.1289 , pp. 252-260
    • Di Simplico, P.1    Lupis, E.2    Rossi, R.3
  • 54
    • 0027092594 scopus 로고
    • The hemoglobins of Notothenia angustata, a temperate fish belonging to a family largely endemic to the Antarctic Ocean
    • A. Fago R. D'Avino G. di Prisco The hemoglobins of Notothenia angustata , a temperate fish belonging to a family largely endemic to the Antarctic Ocean Eur. J. Biochem. 210 1992 963 970
    • (1992) Eur. J. Biochem. , vol.210 , pp. 963-970
    • Fago, A.1    D'Avino, R.2    di Prisco, G.3
  • 55
    • 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. Feurlein L. Sottrup‐Jensen 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    Feurlein, R.J.4    Sottrup‐Jensen, L.5    Weber, R.E.6
  • 56
    • 0031467184 scopus 로고    scopus 로고
    • Temperature‐dependent enthalpy of oxygenation in Antarctic fish hemoglobins
    • A. Fago R.M.G. Wells R.E. Weber Temperature‐dependent enthalpy of oxygenation in Antarctic fish hemoglobins Comp. Biochem. Physiol. 118B 1997 319 326
    • (1997) Comp. Biochem. Physiol. , vol.118B , pp. 319-326
    • Fago, A.1    Wells, R.M.G.2    Weber, R.E.3
  • 57
    • 14244272613 scopus 로고    scopus 로고
    • Hemoglobin and subunit multiplicity in the rainbow trout (Oncorhynchus mykiss) haemoglobin system
    • A. Fago E. Forest R.E. Weber Hemoglobin and subunit multiplicity in the rainbow trout ( Oncorhynchus mykiss ) haemoglobin system Fish Physiol. Biochem. 24 2002 335 342
    • (2002) Fish Physiol. Biochem. , vol.24 , pp. 335-342
    • Fago, A.1    Forest, E.2    Weber, R.E.3
  • 58
    • 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 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. USA 100 2003 12087 12092
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 12087-12092
    • Fago, A.1    Crumbliss, A.L.2    Peterson, J.3    Pearce, L.L.4    Bonaventura, C.5
  • 61
    • 0032445353 scopus 로고    scopus 로고
    • The haemoglobin system of the mudfish, Labeo capensis: Adaptations to temperature and hypoxia
    • B.J. Frey R.E. Weber W.J. van Aardt A. Fago The haemoglobin system of the mudfish, Labeo capensis : Adaptations to temperature and hypoxia Comp. Biochem. Physiol. 120B 1998 735 742
    • (1998) Comp. Biochem. Physiol. , vol.120B , pp. 735-742
    • Frey, B.J.1    Weber, R.E.2    van Aardt, W.J.3    Fago, A.4
  • 64
    • 0000207813 scopus 로고
    • New variants of the haemoglobins of Atlantic cod: A tool for discriminating between coastal and Arctic cod populations
    • U.E.H. Fyhn O. Brix G. Nævdal T. Johansen New variants of the haemoglobins of Atlantic cod: A tool for discriminating between coastal and Arctic cod populations ICES Mar. Sci. Symp. 198 1994 666 670
    • (1994) ICES Mar. Sci. Symp. , vol.198 , pp. 666-670
    • Fyhn, U.E.H.1    Brix, O.2    Nævdal, G.3    Johansen, T.4
  • 65
    • 0029916816 scopus 로고    scopus 로고
    • Multiple hemoglobins in the electric ray: Torpedo marmorata
    • U. Galderisi L. Fucci G. Geraci Multiple hemoglobins in the electric ray: Torpedo marmorata Comp. Biochem. Physiol. 113B 1996 645 651
    • (1996) Comp. Biochem. Physiol. , vol.113B , pp. 645-651
    • Galderisi, U.1    Fucci, L.2    Geraci, G.3
  • 66
    • 34249769205 scopus 로고
    • Experimental control of stress hormone levels in fish: Techniques and applications
    • A.K. Gamperl M.M. Vijayan R.G. Boutilier Experimental control of stress hormone levels in fish: Techniques and applications Rev. Fish Biol. Fisheries 4 1994 215 255
    • (1994) Rev. Fish Biol. Fisheries , vol.4 , pp. 215-255
    • Gamperl, A.K.1    Vijayan, M.M.2    Boutilier, R.G.3
  • 67
    • 7944219982 scopus 로고    scopus 로고
    • The Bohr effect of haemoglobin in vertebrates: An example of molecular adaptation to different physiological requirements
    • B. Giardina D. Mosca M.C. De Rosa The Bohr effect of haemoglobin in vertebrates: An example of molecular adaptation to different physiological requirements Acta Physiol. Scand. 182 2004 229 244
    • (2004) Acta Physiol. Scand. , vol.182 , pp. 229-244
    • Giardina, B.1    Mosca, D.2    De Rosa, M.C.3
  • 68
    • 0008274360 scopus 로고
    • Strain differences in hemoglobin polymorphism, oxygen consumption, and blood oxygen equilibria in three hatchery broodstocks of Arctic charr, Salvelinus alpinus
    • M.A. Giles Strain differences in hemoglobin polymorphism, oxygen consumption, and blood oxygen equilibria in three hatchery broodstocks of Arctic charr, Salvelinus alpinus Fish Physiol. Biochem. 9 1991 291 301
    • (1991) Fish Physiol. Biochem. , vol.9 , pp. 291-301
    • Giles, M.A.1
  • 69
    • 0035852651 scopus 로고    scopus 로고
    • Hypoxia‐induced gene expression profiling in the euryoxic fish Gillichthys mirabilis
    • A.Y. Gracey J.V. Troll G.N. Somero Hypoxia‐induced gene expression profiling in the euryoxic fish Gillichthys mirabilis PNAS 98 2001 1993 1998
    • (2001) PNAS , vol.98 , pp. 1993-1998
    • Gracey, A.Y.1    Troll, J.V.2    Somero, G.N.3
  • 70
    • 85120238516 scopus 로고    scopus 로고
    • J.B. Graham Air‐Breathing Fishes: Evolution, Diversity, and Adaptation. 1997 Academic Press London
    • (1997)
    • Graham, J.B.1
  • 71
    • 0014490512 scopus 로고
    • Temperature‐induced changes in the oxygen equilibrium curve of the blood of the brown bullhead, Ictalurus nebulosus
    • G.C. Grigg Temperature‐induced changes in the oxygen equilibrium curve of the blood of the brown bullhead, Ictalurus nebulosus Comp. Biochem. Physiol. 28 1969 1203 1223
    • (1969) Comp. Biochem. Physiol. , vol.28 , pp. 1203-1223
    • Grigg, G.C.1
  • 72
    • 0036309656 scopus 로고    scopus 로고
    • Myoglobin deficiency in the hearts of phylogenetically diverse temperate‐zone fish species
    • T.J. Grove B.D. Sidell Myoglobin deficiency in the hearts of phylogenetically diverse temperate‐zone fish species Can. J. Zool. 80 2002 893 901
    • (2002) Can. J. Zool. , vol.80 , pp. 893-901
    • Grove, T.J.1    Sidell, B.D.2
  • 73
    • 33645036561 scopus 로고    scopus 로고
    • Oxidative stress and HIF‐1 DNA binding during stressful cold exposure and recovery in the North Sea eelpout (Zoarces viviparus)
    • K. Heise S. Puntarulo M. Nikinmaa M. Lucassen H.‐O. Pörtner D. Abele Oxidative stress and HIF‐1 DNA binding during stressful cold exposure and recovery in the North Sea eelpout ( Zoarces viviparus ) Comp. Biochem. Physiol. 143A 2006 494 503
    • (2006) Comp. Biochem. Physiol. , vol.143A , pp. 494-503
    • Heise, K.1    Puntarulo, S.2    Nikinmaa, M.3    Lucassen, M.4    Pörtner, H.‐O.5    Abele, D.6
  • 74
    • 34548794162 scopus 로고    scopus 로고
    • Effects of seasonal and latitudinal cold on oxidative stress parameters and activation of hypoxia inducible factor (HIF‐1) in zoarcid fish
    • K. Heise M.S. Estevez S. Puntarulo M. Galleano M. Nikinmaa H.O. Pörtner D. Abele Effects of seasonal and latitudinal cold on oxidative stress parameters and activation of hypoxia inducible factor (HIF‐1) in zoarcid fish J. Comp. Physiol. 177B 2007 765 777
    • (2007) J. Comp. Physiol. , vol.177B , pp. 765-777
    • Heise, K.1    Estevez, M.S.2    Puntarulo, S.3    Galleano, M.4    Nikinmaa, M.5    Pörtner, H.O.6    Abele, D.7
  • 75
    • 34748826812 scopus 로고    scopus 로고
    • Characterization of the hemoglobins of the adult brushtailed possum, Trichosurus vulpecula (Kerr) reveals non‐genetic heterogeneity
    • K. Henty R.M.G. Wells T. Brittain Characterization of the hemoglobins of the adult brushtailed possum, Trichosurus vulpecula (Kerr) reveals non‐genetic heterogeneity Comp. Biochem. Physiol. 148A 2007 498 503
    • (2007) Comp. Biochem. Physiol. , vol.148A , pp. 498-503
    • Henty, K.1    Wells, R.M.G.2    Brittain, T.3
  • 76
    • 0036937389 scopus 로고    scopus 로고
    • The effect of strenuous exercise and β‐adrenergic blockade on the visual performance of juvenile rainbow trout, Oncorhynchus mykiss
    • N.A. Herbert R.M.G. Wells The effect of strenuous exercise and β‐adrenergic blockade on the visual performance of juvenile rainbow trout, Oncorhynchus mykiss J. Comp. Physiol. 172B 2002 725 731
    • (2002) J. Comp. Physiol. , vol.172B , pp. 725-731
    • Herbert, N.A.1    Wells, R.M.G.2
  • 77
    • 0037125680 scopus 로고    scopus 로고
    • Correlates of choroid rete development with the metabolic potential of various tropical reef fish and the effect of strenuous exercise on visual performance
    • N.A. Herbert R.M.G. Wells J. Baldwin Correlates of choroid rete development with the metabolic potential of various tropical reef fish and the effect of strenuous exercise on visual performance J. Exp. Mar. Biol. Ecol. 275 2002 31 46
    • (2002) J. Exp. Mar. Biol. Ecol. , vol.275 , pp. 31-46
    • Herbert, N.A.1    Wells, R.M.G.2    Baldwin, J.3
  • 78
    • 33748776834 scopus 로고    scopus 로고
    • Whole blood‐oxygen binding properties of four cold‐temperate marine fishes: Blood affinity is independent of pH‐dependent binding, routine swimming performance, and environmental hypoxia
    • N.A. Herbert P.V. Skov R.M.G. Wells J.F. Steffensen Whole blood‐oxygen binding properties of four cold‐temperate marine fishes: Blood affinity is independent of pH‐dependent binding, routine swimming performance, and environmental hypoxia Physiol. Biochem. Zool. 79 2006 909 918
    • (2006) Physiol. Biochem. Zool. , vol.79 , pp. 909-918
    • Herbert, N.A.1    Skov, P.V.2    Wells, R.M.G.3    Steffensen, J.F.4
  • 80
    • 0028253750 scopus 로고
    • Variable versus constant temperature acclimation regimes: Effects on hemoglobin isomorph profile in goldfish, Carassius auratus
    • A.H. Houston J.H. Gingras‐Bedard Variable versus constant temperature acclimation regimes: Effects on hemoglobin isomorph profile in goldfish, Carassius auratus Fish Physiol. Biochem. 13 1994 445 450
    • (1994) Fish Physiol. Biochem. , vol.13 , pp. 445-450
    • Houston, A.H.1    Gingras‐Bedard, J.H.2
  • 81
    • 0242322032 scopus 로고    scopus 로고
    • Allosteric effect of water in fish and human hemoglobins
    • C. Hundahl A. Fago H. Malte 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
  • 84
    • 0021104746 scopus 로고
    • Oxygen equilibrium studies on hemoglobin from the bluefin tuna (Thunnus thynnus)
    • M. Ikeda‐Saito T. Yonetani 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
  • 85
    • 0033677397 scopus 로고    scopus 로고
    • Hemoglobin genotypes of turbot (Scophthalamus maximus): Consequences for growth and variations in optimal temperature for growth
    • A.K. Imsland A. Foss S.O. Stefansson G. Nævdal Hemoglobin genotypes of turbot ( Scophthalamus maximus ): Consequences for growth and variations in optimal temperature for growth Fish Physiol. Biochem. 23 2000 75 81
    • (2000) Fish Physiol. Biochem. , vol.23 , pp. 75-81
    • Imsland, A.K.1    Foss, A.2    Stefansson, S.O.3    Nævdal, G.4
  • 86
    • 0036786408 scopus 로고    scopus 로고
    • Influence of hypoxia and hypoxemia on the development of cardiac activity in zebrafish larvae
    • E. Jacob M. Drexel T. Schwerte B. Pelster Influence of hypoxia and hypoxemia on the development of cardiac activity in zebrafish larvae Amer. J. Physiol. 283 2002 R911 R917
    • (2002) Amer. J. Physiol. , vol.283 , pp. R911-R917
    • Jacob, E.1    Drexel, M.2    Schwerte, T.3    Pelster, B.4
  • 88
    • 0024670912 scopus 로고
    • Hydrogen ion equilibria in fish haemoglobins
    • F.B. Jensen Hydrogen ion equilibria in fish haemoglobins J. Exp. Biol. 143 1989 225 234
    • (1989) J. Exp. Biol. , vol.143 , pp. 225-234
    • Jensen, F.B.1
  • 89
    • 0034967869 scopus 로고    scopus 로고
    • Hydrogen ion binding properties of tuna haemoglobins
    • F.B. Jensen Hydrogen ion binding properties of tuna haemoglobins Comp. Biochem. Physiol. 129A 2001 511 517
    • (2001) Comp. Biochem. Physiol. , vol.129A , pp. 511-517
    • Jensen, F.B.1
  • 90
    • 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. 135A 2003 9 24
    • (2003) Comp. Biochem. Physiol. , vol.135A , pp. 9-24
    • Jensen, F.B.1
  • 91
    • 7944237674 scopus 로고    scopus 로고
    • Red blood cell pH, the Bohr effect, and other oxygenation‐linked phenomena in blood O2 and CO2 transport
    • 2 transport Acta Physiol. Scand. 182 2004 215 227
    • (2004) Acta Physiol. Scand. , vol.182 , pp. 215-227
    • Jensen, F.B.1
  • 92
    • 44949238560 scopus 로고    scopus 로고
    • Nitric oxide formation from the reaction of nitrite with carp and rabbit haemoglobin at intermediate oxygen saturations
    • F.B. Jensen Nitric oxide formation from the reaction of nitrite with carp and rabbit haemoglobin at intermediate oxygen saturations FEBS Journal 275 2008 3375 3387
    • (2008) FEBS Journal , vol.275 , pp. 3375-3387
    • Jensen, F.B.1
  • 93
    • 0020375415 scopus 로고
    • Respiratory properties of tench blood and hemoglobin adaptations to hypoxic‐hypercapnic water
    • F.B. Jensen R.E. Weber Respiratory properties of tench blood and hemoglobin adaptations to hypoxic‐hypercapnic water Mol. Physiol. 2 1982 235 250
    • (1982) Mol. Physiol. , vol.2 , pp. 235-250
    • Jensen, F.B.1    Weber, R.E.2
  • 94
    • 0001694288 scopus 로고
    • Environmental perturbations of oxygen transport in teleost fishes: Causes, consequences, and compensations
    • F.B. Jensen M. Nikinmaa R.E. Weber Environmental perturbations of oxygen transport in teleost fishes: Causes, consequences, and compensations J.C. Rankin F.B. Jensen Fish Ecophysiology 1993 Chapman and Hall London 161 179
    • (1993) , pp. 161-179
    • Jensen, F.B.1    Nikinmaa, M.2    Weber, R.E.3
  • 95
    • 77956747884 scopus 로고    scopus 로고
    • Hemoglobin structure and function
    • F.B. Jensen A. Fago R.E. Weber Hemoglobin structure and function S.F. Perry B.L. Tufts Fish Physiology Vol. 17 1998 Academic Press San Diego 1 40
    • (1998) , pp. 1-40
    • Jensen, F.B.1    Fago, A.2    Weber, R.E.3
  • 96
    • 0017139997 scopus 로고
    • Respiratory properties of blood in awake and estivating lungfish, Protopterus amphibius
    • K. Johansen G. Lykkeboe R.E. Weber G.M.O. Maloiy Respiratory properties of blood in awake and estivating lungfish, Protopterus amphibius Resp. Physiol. 27 1976 335 345
    • (1976) Resp. Physiol. , vol.27 , pp. 335-345
    • Johansen, K.1    Lykkeboe, G.2    Weber, R.E.3    Maloiy, G.M.O.4
  • 97
    • 0031450207 scopus 로고    scopus 로고
    • Anoxic depression of light‐evoked potentials in retina and optic tectum of crucian carp
    • D. Johansson G.E. Nilsson B. Døvink Anoxic depression of light‐evoked potentials in retina and optic tectum of crucian carp Neurosci. Letts 237 1997 73 76
    • (1997) Neurosci. Letts , vol.237 , pp. 73-76
    • Johansson, D.1    Nilsson, G.E.2    Døvink, B.3
  • 98
    • 0022616234 scopus 로고
    • The influence of blood gas properties on gas tensions and pH of ventral and dorsal aortic blood in free‐swimming tuna, Euthynnus affinis
    • D.R. Jones R.W. Brill D.C. Mense The influence of blood gas properties on gas tensions and pH of ventral and dorsal aortic blood in free‐swimming tuna, Euthynnus affinis J. Exp. Biol. 120 1986 201 213
    • (1986) J. Exp. Biol. , vol.120 , pp. 201-213
    • Jones, D.R.1    Brill, R.W.2    Mense, D.C.3
  • 99
    • 34547819199 scopus 로고    scopus 로고
    • Effects of temperature and carbon dioxide on green sturgeon blood‐oxygen equilibrium
    • R.C. Kauffman A.G. Houck J.J. Cech Effects of temperature and carbon dioxide on green sturgeon blood‐oxygen equilibrium Environ. Biol. Fish 79 2007 201 210
    • (2007) Environ. Biol. Fish , vol.79 , pp. 201-210
    • Kauffman, R.C.1    Houck, A.G.2    Cech, J.J.3
  • 100
    • 0039099826 scopus 로고
    • Blood physiology and ecological consequences in Weddell Sea fishes (Antarctica)
    • A. Kunzmann Blood physiology and ecological consequences in Weddell Sea fishes (Antarctica) Berichte zur Polarforschung 91 1991 1 79
    • (1991) Berichte zur Polarforschung , vol.91 , pp. 1-79
    • Kunzmann, A.1
  • 101
    • 33747034989 scopus 로고    scopus 로고
    • Effects of moderate and substantial hypoxia on erythropoietin levels in rainbow trout kidney and spleen
    • J.C.C. Lai I. Kakuta H.O.L. Mok J.L. Rummer D. Randall Effects of moderate and substantial hypoxia on erythropoietin levels in rainbow trout kidney and spleen J. Exp. Biol. 209 2006 2734 2738
    • (2006) J. Exp. Biol. , vol.209 , pp. 2734-2738
    • Lai, J.C.C.1    Kakuta, I.2    Mok, H.O.L.3    Rummer, J.L.4    Randall, D.5
  • 102
    • 0042232406 scopus 로고    scopus 로고
    • ATP‐induced reverse temperature effect in isohemoglobins from the endothermic porbeagle shark (Lamna nasus)
    • C. Larsen H. Malte R.E. Weber ATP‐induced reverse temperature effect in isohemoglobins 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
  • 103
    • 0032827079 scopus 로고    scopus 로고
    • Seasonal and temperature effects on the adrenergic responses of Arctic charr (Salvelinus alpinus) erythrocytes
    • T. Lecklin M. Nikinmaa Seasonal and temperature effects on the adrenergic responses of Arctic charr ( Salvelinus alpinus ) erythrocytes J. Exp. Biol. 202 1999 2233 2238
    • (1999) J. Exp. Biol. , vol.202 , pp. 2233-2238
    • Lecklin, T.1    Nikinmaa, M.2
  • 104
    • 0030221951 scopus 로고    scopus 로고
    • Primary and secondary stress responses to line capture in the blue mao mao
    • T.E. Lowe R.M.G. Wells Primary and secondary stress responses to line capture in the blue mao mao J. Fish Biol. 49 1996 287 300
    • (1996) J. Fish Biol. , vol.49 , pp. 287-300
    • Lowe, T.E.1    Wells, R.M.G.2
  • 105
    • 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
    • T.E. Lowe R.W. Brill K.L. Cousins 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. 168B 1998 405 418
    • (1998) J. Comp. Physiol. , vol.168B , pp. 405-418
    • Lowe, T.E.1    Brill, R.W.2    Cousins, K.L.3
  • 106
    • 0000358901 scopus 로고    scopus 로고
    • Blood oxygen‐binding characteristics of bigeye tuna (Thunnus obesus), a high‐energy‐demand teleost that is tolerant of low oxygen
    • T.E. Lowe R.W. Brill K.L. Cousins Blood oxygen‐binding characteristics of bigeye tuna ( Thunnus obesus ), a high‐energy‐demand teleost that is tolerant of low oxygen Mar. Biol. 136 2000 1087 1098
    • (2000) Mar. Biol. , vol.136 , pp. 1087-1098
    • Lowe, T.E.1    Brill, R.W.2    Cousins, K.L.3
  • 107
    • 0017993883 scopus 로고
    • Ecological peculiarities of hemoglobinograms of three species of sturgeons
    • V.I. Luk'yanenko Ecological peculiarities of hemoglobinograms of three species of sturgeons Zh. Evol. Biokhim. Fiziol. 14 1978 347 350
    • (1978) Zh. Evol. Biokhim. Fiziol. , vol.14 , pp. 347-350
    • Luk'yanenko, V.I.1
  • 108
    • 34748849521 scopus 로고    scopus 로고
    • Molecular characterisation and expression of Atlantic cod (Gadus morhua) myoglobin from two populations held at two different acclimation temperatures
    • G.J. Lurman N. Koschnick H‐O. Pörtner M. Lucassen Molecular characterisation and expression of Atlantic cod ( Gadus morhua ) myoglobin from two populations held at two different acclimation temperatures Comp. Biochem. Physiol. 148A 2007 681 689
    • (2007) Comp. Biochem. Physiol. , vol.148A , pp. 681-689
    • Lurman, G.J.1    Koschnick, N.2    Pörtner, H‐O.3    Lucassen, M.4
  • 109
    • 0035021860 scopus 로고    scopus 로고
    • Oxygen affinity and amino acid sequence of myoglobins from endothermic and ectothermic fish
    • B.J. Marcinek J. Bonaventura J.B. Wittenberg B.A. Block Oxygen affinity and amino acid sequence of myoglobins from endothermic and ectothermic fish Am. J. Physiol. 280 2001 R1123 R1133
    • (2001) Am. J. Physiol. , vol.280 , pp. R1123-R1133
    • Marcinek, B.J.1    Bonaventura, J.2    Wittenberg, J.B.3    Block, B.A.4
  • 110
    • 0141592328 scopus 로고    scopus 로고
    • Unique features of the haemoglobin system of the Antarctic notothenioid fish Gobionotothen gibberifrons
    • P. Marinakis M. Tamburrini V. Carratore G. di Prisco Unique features of the haemoglobin system of the Antarctic notothenioid fish Gobionotothen gibberifrons Eur. J. Biochem. 270 2003 3981 3987
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3981-3987
    • Marinakis, P.1    Tamburrini, M.2    Carratore, V.3    di Prisco, G.4
  • 111
    • 0000525169 scopus 로고
    • Effect of hypoxia on haemoglobin isomorph abundances in rainbow trout, Salmo gairdneri
    • C.A. Marinsky A.H. Houston A. Murad Effect of hypoxia on haemoglobin isomorph abundances in rainbow trout, Salmo gairdneri Can. J. Zool. 68 1990 884 888
    • (1990) Can. J. Zool. , vol.68 , pp. 884-888
    • Marinsky, C.A.1    Houston, A.H.2    Murad, A.3
  • 112
    • 8444238299 scopus 로고    scopus 로고
    • The effects of sustained exercise and hypoxia upon oxygen tensions in the red muscle of rainbow trout
    • D.J. McKenzie S. Wong D.J. Randall S. Egginton E.W. Taylor A.P. Farrell The effects of sustained exercise and hypoxia upon oxygen tensions in the red muscle of rainbow trout J. Exp. Biol. 207 2004 3629 3637
    • (2004) J. Exp. Biol. , vol.207 , pp. 3629-3637
    • McKenzie, D.J.1    Wong, S.2    Randall, D.J.3    Egginton, S.4    Taylor, E.W.5    Farrell, A.P.6
  • 113
    • 0038035496 scopus 로고    scopus 로고
    • Water regulates oxygen binding in hagfish (Myxine glutinosa) haemoglobin
    • G. Müller A. Fago R.E. Weber Water regulates oxygen binding in hagfish ( Myxine glutinosa ) haemoglobin 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
  • 114
    • 0011689871 scopus 로고
    • Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli
    • K. Nagai M.F. Perutz C. Poyart Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli Proc. Natl Acad. Sci. USA 82 1985 7252 7255
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 7252-7255
    • Nagai, K.1    Perutz, M.F.2    Poyart, C.3
  • 115
    • 0024350819 scopus 로고
    • Comparative oxygen affinity of fish and mammalian myoglobins
    • J.W. Nichols L.J. Weber Comparative oxygen affinity of fish and mammalian myoglobins J. Comp. Physiol. 159B 1989 205 209
    • (1989) J. Comp. Physiol. , vol.159B , pp. 205-209
    • Nichols, J.W.1    Weber, L.J.2
  • 117
    • 0020381755 scopus 로고
    • Effects of adrenaline on red cell volume and concentration gradient of protons across the red cell membrane in the rainbow trout, Salmo gardneri
    • M. Nikinmaa Effects of adrenaline on red cell volume and concentration gradient of protons across the red cell membrane in the rainbow trout, Salmo gardneri Mol. Physiol. 2 1982 287 297
    • (1982) Mol. Physiol. , vol.2 , pp. 287-297
    • Nikinmaa, M.1
  • 118
    • 34250154793 scopus 로고
    • Adrenergic regulation of haemoglobin oxygen affinity in rainbow trout cells
    • M. Nikinmaa Adrenergic regulation of haemoglobin oxygen affinity in rainbow trout cells J. Comp. Physiol. 152B 1983 67 72
    • (1983) J. Comp. Physiol. , vol.152B , pp. 67-72
    • Nikinmaa, M.1
  • 119
    • 0030901801 scopus 로고    scopus 로고
    • Oxygen and carbon dioxide transport in vertebrate erythrocytes: An evolutionary change in the role of membrane transport
    • M. Nikinmaa Oxygen and carbon dioxide transport in vertebrate erythrocytes: An evolutionary change in the role of membrane transport J. Exp. Biol. 200 1997 369 380
    • (1997) J. Exp. Biol. , vol.200 , pp. 369-380
    • Nikinmaa, M.1
  • 120
    • 0035173739 scopus 로고    scopus 로고
    • Haemoglobin function in vertebrates: Evolutionary changes in cellular regulation in hypoxia
    • M. Nikinmaa Haemoglobin function in vertebrates: Evolutionary changes in cellular regulation in hypoxia Respir. Physiol. 128 2001 317 329
    • (2001) Respir. Physiol. , vol.128 , pp. 317-329
    • Nikinmaa, M.1
  • 121
    • 0036024287 scopus 로고    scopus 로고
    • Oxygen‐dependent cellular functions – why fish and their aquatic environment are a prime choice of study
    • M. Nikinmaa Oxygen‐dependent cellular functions – why fish and their aquatic environment are a prime choice of study Comp. Biochem. Physiol. 133A 2002 1 16
    • (2002) Comp. Biochem. Physiol. , vol.133A , pp. 1-16
    • Nikinmaa, M.1
  • 122
    • 0042420536 scopus 로고    scopus 로고
    • β3‐Adrenergic receptors – studies on rainbow trout reveal ancient evolutionary origins and functions distinct from the thermogenic response
    • 3‐Adrenergic receptors – studies on rainbow trout reveal ancient evolutionary origins and functions distinct from the thermogenic response Am. J. Physiol. 285 2003 R515 R516
    • (2003) Am. J. Physiol. , vol.285 , pp. R515-R516
    • Nikinmaa, M.1
  • 123
    • 7944221969 scopus 로고    scopus 로고
    • The Bohr effect – a discovery 100 years ago, with intensive studies about the effect of protons on haemoglobins still going on
    • M. Nikinmaa The Bohr effect – a discovery 100 years ago, with intensive studies about the effect of protons on haemoglobins still going on Acta Physiol. Scand. 182 2004 213 214
    • (2004) Acta Physiol. Scand. , vol.182 , pp. 213-214
    • Nikinmaa, M.1
  • 124
    • 85120193013 scopus 로고    scopus 로고
    • Gas transport
    • M. Nikinmaa Gas transport D.H. Evans J.B. Claiborne The Physiology of Fishes 3rd edn 2006 CRC Press, Taylor and Francis Boca Raton, FL 153 174
    • (2006) , pp. 153-174
    • Nikinmaa, M.1
  • 125
    • 0021699932 scopus 로고
    • Adrenergic swelling in nucleated erythrocytes: Cellular mechanisms in a bird, domestic goose, and two teleosts, striped bass and rainbow trout
    • M. Nikinmaa W.H. Heustis Adrenergic swelling in nucleated erythrocytes: Cellular mechanisms in a bird, domestic goose, and two teleosts, striped bass and rainbow trout J. Exp. Biol. 113 1984 215 224
    • (1984) J. Exp. Biol. , vol.113 , pp. 215-224
    • Nikinmaa, M.1    Heustis, W.H.2
  • 126
    • 17844372978 scopus 로고    scopus 로고
    • Oxygen‐dependent gene expression in fishes
    • M. Nikinmaa R.B. Rees Oxygen‐dependent gene expression in fishes Amer. J. Physiol. 288 2005 R1079 R1090
    • (2005) Amer. J. Physiol. , vol.288 , pp. R1079-R1090
    • Nikinmaa, M.1    Rees, R.B.2
  • 127
    • 0001282250 scopus 로고
    • Blood oxygen transport in stressed striped bass (Morone saxatilis): Role of β‐adrenergic responses
    • M. Nikinmaa J.J. Cech M. McEnroe Blood oxygen transport in stressed striped bass ( Morone saxatilis ): Role of β‐adrenergic responses J. Comp. Physiol. 154B 1984 365 369
    • (1984) J. Comp. Physiol. , vol.154B , pp. 365-369
    • Nikinmaa, M.1    Cech, J.J.2    McEnroe, M.3
  • 128
    • 0035060611 scopus 로고    scopus 로고
    • β‐Adrenergic stimulation of volume‐sensitive chloride transport in lamprey erythrocytes
    • M. Nikinmaa A. Salama A. Bogdanova L.V. Virkki β‐Adrenergic stimulation of volume‐sensitive chloride transport in lamprey erythrocytes Physiol. Biochem. Zool. 74 2001 45 51
    • (2001) Physiol. Biochem. Zool. , vol.74 , pp. 45-51
    • Nikinmaa, M.1    Salama, A.2    Bogdanova, A.3    Virkki, L.V.4
  • 129
    • 0035489396 scopus 로고    scopus 로고
    • Surviving anoxia with the brain turned on
    • G.E. Nilsson Surviving anoxia with the brain turned on News Physiol. Sci. 16 2001 217 221
    • (2001) News Physiol. Sci. , vol.16 , pp. 217-221
    • Nilsson, G.E.1
  • 130
    • 85120215672 scopus 로고    scopus 로고
    • Hypoxia tolerance in coral reef fishes
    • G.E. Nilsson S. Östlund‐Nilsson Hypoxia tolerance in coral reef fishes A.L. Val V.M.F. de Almeida‐Val D.J. Randall The Physiology of Tropical Fishes W.S. Hoar D.J. Randall A.P. Farrell Fish Physiology Vol. 21 2006 Academic Press London 583 596
    • (2006) , pp. 583-596
    • Nilsson, G.E.1    Östlund‐Nilsson, S.2
  • 131
    • 4644324293 scopus 로고    scopus 로고
    • Hypoxic survival strategies in two fishes: Extreme anoxia tolerance in the North European crucian carp and natural hypoxic preconditioning in a coral‐reef shark
    • G.E. Nilsson G.M.C. Renshaw Hypoxic survival strategies in two fishes: Extreme anoxia tolerance in the North European crucian carp and natural hypoxic preconditioning in a coral‐reef shark J. Exp. Biol. 207 2004 3131 3139
    • (2004) J. Exp. Biol. , vol.207 , pp. 3131-3139
    • Nilsson, G.E.1    Renshaw, G.M.C.2
  • 132
    • 0033952927 scopus 로고    scopus 로고
    • Increased glutathionyl haemoglobin in diabetes mellitus and hyperlipidemia demonstrated by liquid chromatography/electrospray ionization‐mass spectrometry
    • T. Niwa C. Naito A.H. Mawjood K. Imai Increased glutathionyl haemoglobin in diabetes mellitus and hyperlipidemia demonstrated by liquid chromatography/electrospray ionization‐mass spectrometry Clin. Chem. 46 2000 399 419
    • (2000) Clin. Chem. , vol.46 , pp. 399-419
    • Niwa, T.1    Naito, C.2    Mawjood, A.H.3    Imai, K.4
  • 134
    • 0037591730 scopus 로고    scopus 로고
    • Structural‐functional characterization of the cathodal hemoglobin of the conger eel Conger conger: Molecular modelling study of an additional phosphate‐binding site
    • M. Pellegrini B. Giardina C. Verde V. Carratore A. Olianas L. Sollai M.T. Sanna M. Castagnola G. di Prisco Structural‐functional characterization of the cathodal hemoglobin of the conger eel Conger conger : Molecular modelling study of an additional phosphate‐binding site Biochem. J. 372 2003 679 686
    • (2003) Biochem. J. , vol.372 , pp. 679-686
    • Pellegrini, M.1    Giardina, B.2    Verde, C.3    Carratore, V.4    Olianas, A.5    Sollai, L.6    Sanna, M.T.7    Castagnola, M.8    di Prisco, G.9
  • 135
    • 0035999610 scopus 로고    scopus 로고
    • Nitric oxide‐cGMP‐mediated vasoconstriction and effects of acetylcholine in the branchial circulation of the eel
    • D. Pellegrino E. Sprovieri R. Mazza D.J. Randall B. Tota Nitric oxide‐cGMP‐mediated vasoconstriction and effects of acetylcholine in the branchial circulation of the eel Comp. Biochem. Physiol. 132A 2002 447 457
    • (2002) Comp. Biochem. Physiol. , vol.132A , pp. 447-457
    • Pellegrino, D.1    Sprovieri, E.2    Mazza, R.3    Randall, D.J.4    Tota, B.5
  • 136
    • 10444289869 scopus 로고    scopus 로고
    • No hemoglobin but NO: The icefish (Chionodraco hamatus) heart as a paradigm
    • D. Pellegrino C.A. Palmerini B. Tota No hemoglobin but NO: The icefish ( Chionodraco hamatus ) heart as a paradigm J. Exp. Biol. 207 2004 3855 3864
    • (2004) J. Exp. Biol. , vol.207 , pp. 3855-3864
    • Pellegrino, D.1    Palmerini, C.A.2    Tota, B.3
  • 137
    • 33645144963 scopus 로고    scopus 로고
    • The physiology of the Root effect
    • B. Pelster D. Randall The physiology of the Root effect S.F. Perry B.L. Tufts Fish Physiology Vol. 17 1998 Academic Press London 113 139
    • (1998) , pp. 113-139
    • Pelster, B.1    Randall, D.2
  • 138
    • 0025289366 scopus 로고
    • Influence of organic phosphates on the Root effect of multiple fish haemoglobins
    • B. Pelster R.E. Weber Influence of organic phosphates on the Root effect of multiple fish haemoglobins J. Exp. Biol. 149 1990 425 437
    • (1990) J. Exp. Biol. , vol.149 , pp. 425-437
    • Pelster, B.1    Weber, R.E.2
  • 140
    • 0026903684 scopus 로고
    • Relationship between blood O2 content and catecholamine levels during hypoxia in rainbow trout and American eel
    • 2 content and catecholamine levels during hypoxia in rainbow trout and American eel Am. J. Physiol. 263 1992 R240 R249
    • (1992) Am. J. Physiol. , vol.263 , pp. R240-R249
    • Perry, S.F.1    Reid, S.D.2
  • 141
    • 2642568632 scopus 로고    scopus 로고
    • A comparative study of blood oxygen transport in turbot and sea bass: Effect of chronic hypoxia
    • K. Pichavant V. Maxime P. Soulier G. Boeuf G. Nonnotte A comparative study of blood oxygen transport in turbot and sea bass: Effect of chronic hypoxia J. Fish Biol. 62 2003 928 937
    • (2003) J. Fish Biol. , vol.62 , pp. 928-937
    • Pichavant, K.1    Maxime, V.2    Soulier, P.3    Boeuf, G.4    Nonnotte, G.5
  • 142
    • 0001307368 scopus 로고
    • Cardiac growth, myoglobin proteins and DNA in developing tuna (Thunnus thynnus thynnus L.)
    • O. Poupa L. Lindström A. Maresca B. Tota Cardiac growth, myoglobin proteins and DNA in developing tuna ( Thunnus thynnus thynnus L.) Comp. Biochem. Physiol. 70A 1981 217 222
    • (1981) Comp. Biochem. Physiol. , vol.70A , pp. 217-222
    • Poupa, O.1    Lindström, L.2    Maresca, A.3    Tota, B.4
  • 143
    • 0018409275 scopus 로고
    • The effect of temperature on the oxygen equilibria of fish hemoglobins in relation to environmental thermal variability
    • D.A. Powers J.P. Martin R.L. Garlick H.J. Fyhn U.E.H. Fyhn The effect of temperature on the oxygen equilibria of fish hemoglobins in relation to environmental thermal variability Comp. Biochem. Physiol. 62A 1979 87 94
    • (1979) Comp. Biochem. Physiol. , vol.62A , pp. 87-94
    • Powers, D.A.1    Martin, J.P.2    Garlick, R.L.3    Fyhn, H.J.4    Fyhn, U.E.H.5
  • 144
    • 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 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
  • 146
    • 85117395490 scopus 로고
    • Catecholamines
    • D.J. Randall S.F. Perry Catecholamines W.S. Hoar D.J. Randall A.P. Farrell Fish Physiology Vol. 12B 1992 Academic Press London 255 300
    • (1992) , pp. 255-300
    • Randall, D.J.1    Perry, S.F.2
  • 147
    • 85120222958 scopus 로고    scopus 로고
    • Response of aquatic vertebrates to hypoxia
    • D.J. Randall C.Y. Hung W.L. Poon Response of aquatic vertebrates to hypoxia D.J. Randall D.Y.M. Mandy Fish Physiology, Toxicology, and Water Quality 2006 Ecosystems Research Division Athens, GA 1 10
    • (2006) , pp. 1-10
    • Randall, D.J.1    Hung, C.Y.2    Poon, W.L.3
  • 148
    • 34447341171 scopus 로고    scopus 로고
    • Distribution, adaptation and physiological meaning of thiols from vertebrate hemoglobins
    • E. Reischl A.L. Dafre F.L. Franco D. Wilhelm Filho Distribution, adaptation and physiological meaning of thiols from vertebrate hemoglobins Comp. Biochem. Physiol. 146C 2007 22 53
    • (2007) Comp. Biochem. Physiol. , vol.146C , pp. 22-53
    • Reischl, E.1    Dafre, A.L.2    Franco, F.L.3    Wilhelm Filho, D.4
  • 149
    • 0034533352 scopus 로고    scopus 로고
    • Functionally distinct haemoglobins of the cryopelagic Antarctic teleost Pagothenia borchgrevinki
    • A. Riccio M. Tamburrini V. Carratore G. di Prisco Functionally distinct haemoglobins of the cryopelagic Antarctic teleost Pagothenia borchgrevinki J. Fish Biol. 57 Suppl. A 2000 20 32
    • (2000) J. Fish Biol. , vol.57 , Issue.Suppl. A , pp. 20-32
    • Riccio, A.1    Tamburrini, M.2    Carratore, V.3    di Prisco, G.4
  • 150
    • 33645778794 scopus 로고    scopus 로고
    • Temperature regulates hypoxia‐inducible factor‐1 (HIF‐1) in a poikilothermic vertebrate, crucian carp (Carassius carassius)
    • E. Rissanen H.K. Tranberg J. Sollid G.E. Nilsson M. Nikinmaa Temperature regulates hypoxia‐inducible factor‐1 (HIF‐1) in a poikilothermic vertebrate, crucian carp ( Carassius carassius ) J. Exp. Biol. 209 2006 994 1003
    • (2006) J. Exp. Biol. , vol.209 , pp. 994-1003
    • Rissanen, E.1    Tranberg, H.K.2    Sollid, J.3    Nilsson, G.E.4    Nikinmaa, M.5
  • 151
    • 10344243985 scopus 로고    scopus 로고
    • A globin gene of ancient evolutionary origin in lower vertebrates: Evidence for two distinct globin families in animals
    • A. Roesner C. Fuchs T. Hankeln T. Burmester A globin gene of ancient evolutionary origin in lower vertebrates: Evidence for two distinct globin families in animals Mol. Biol. Evol. 22 2005 12 22
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 12-22
    • Roesner, A.1    Fuchs, C.2    Hankeln, T.3    Burmester, T.4
  • 152
    • 33745616788 scopus 로고    scopus 로고
    • Hypoxia induces a complex response of globin expression in zebrafish (Danio rerio)
    • A. Roesner T. Hankeln T. Burmester Hypoxia induces a complex response of globin expression in zebrafish ( Danio rerio ) J. Exp. Biol. 209 2006 2129 2137
    • (2006) J. Exp. Biol. , vol.209 , pp. 2129-2137
    • Roesner, A.1    Hankeln, T.2    Burmester, T.3
  • 153
    • 50549094066 scopus 로고    scopus 로고
    • Globins and hypoxia in the goldfish, Carassius auratus
    • A. Roesner S.A. Mitz T. Hankeln T. Burmester Globins and hypoxia in the goldfish, Carassius auratus FEBS Journal 275 2008 3633 3643
    • (2008) FEBS Journal , vol.275 , pp. 3633-3643
    • Roesner, A.1    Mitz, S.A.2    Hankeln, T.3    Burmester, T.4
  • 154
    • 34548439777 scopus 로고    scopus 로고
    • Multiple strategies of Lake Victoria cichlids to cope with lifelong hypoxia include hemoglobin switching
    • H.A. Rutjes M.C. Nieveen R.E. Weber F. Witte G.E.E.J.M. Van den Thillart Multiple strategies of Lake Victoria cichlids to cope with lifelong hypoxia include hemoglobin switching Am. J. Physiol. 293 2007 R1376 R1383
    • (2007) Am. J. Physiol. , vol.293 , pp. R1376-R1383
    • Rutjes, H.A.1    Nieveen, M.C.2    Weber, R.E.3    Witte, F.4    Van den Thillart, G.E.E.J.M.5
  • 155
    • 34247473555 scopus 로고    scopus 로고
    • Comparison of hypoxia‐inducible factor‐1 alpha in hypoxia‐sensitive and hypoxia‐tolerant fish species
    • K.T. Rytkönen K.A.M. Vuori C.R. Primmer M. Nikinmaa Comparison of hypoxia‐inducible factor‐1 alpha in hypoxia‐sensitive and hypoxia‐tolerant fish species Comp. Biochem. Physiol. 2D 2007 177 186
    • (2007) Comp. Biochem. Physiol. , vol.2D , pp. 177-186
    • Rytkönen, K.T.1    Vuori, K.A.M.2    Primmer, C.R.3    Nikinmaa, M.4
  • 156
    • 0000405782 scopus 로고    scopus 로고
    • Oxygen binding properties of three different hemoglobin genotypes in turbot (Scophthalamus maximus Rafinesque): Effect of temperature and pH
    • E.N. Samuelsen A.K. Imsland O. Brix Oxygen binding properties of three different hemoglobin genotypes in turbot ( Scophthalamus maximus Rafinesque): Effect of temperature and pH Fish Physiol. Biochem. 20 1999 135 141
    • (1999) Fish Physiol. Biochem. , vol.20 , pp. 135-141
    • Samuelsen, E.N.1    Imsland, A.K.2    Brix, O.3
  • 157
    • 0031424848 scopus 로고    scopus 로고
    • Hemoglobin polymorphism in the Atlantic croaker, Micropogon undulatus
    • D.A. Shelly C.P. Mangum Hemoglobin polymorphism in the Atlantic croaker, Micropogon undulatus Comp. Biochem. Physiol. 118B 1997 1419 1428
    • (1997) Comp. Biochem. Physiol. , vol.118B , pp. 1419-1428
    • Shelly, D.A.1    Mangum, C.P.2
  • 158
    • 33745651826 scopus 로고    scopus 로고
    • When bad things happen to good fish: The loss of haemoglobin and myoglobin expression in Antarctic icefishes
    • B.D. Sidell K.M. O'Brien When bad things happen to good fish: The loss of haemoglobin and myoglobin expression in Antarctic icefishes J. Exp. Biol. 209 2006 1791 1802
    • (2006) J. Exp. Biol. , vol.209 , pp. 1791-1802
    • Sidell, B.D.1    O'Brien, K.M.2
  • 159
    • 0036441640 scopus 로고    scopus 로고
    • Peculiarities of structure, polymorphism, and resistance to oxidation of fish hemoglobins
    • A.A. Soldatov Peculiarities of structure, polymorphism, and resistance to oxidation of fish hemoglobins J. Evol. Biochem. Physiol. 38 2002 392 400
    • (2002) J. Evol. Biochem. Physiol. , vol.38 , pp. 392-400
    • Soldatov, A.A.1
  • 160
    • 17244377098 scopus 로고    scopus 로고
    • Temperature alters the respiratory surface area of crucian carp Carassius carassius and goldfish Carassius auratus
    • J. Sollid R.E. Weber G.E. Nilsson Temperature alters the respiratory surface area of crucian carp Carassius carassius and goldfish Carassius auratus J. Exp. Biol. 208 2005 1109 1116
    • (2005) J. Exp. Biol. , vol.208 , pp. 1109-1116
    • Sollid, J.1    Weber, R.E.2    Nilsson, G.E.3
  • 162
    • 14844303424 scopus 로고    scopus 로고
    • Nitric oxide (NO) in normal and hypoxic vascular regulation of the spiny dogfish, Squalus acanthias
    • K.E. Swenson R.L. Eveland M.T. Gladwin E.R. Swenson Nitric oxide (NO) in normal and hypoxic vascular regulation of the spiny dogfish, Squalus acanthias J. Exp. Zool. 303A 2005 154 160
    • (2005) J. Exp. Zool. , vol.303A , pp. 154-160
    • Swenson, K.E.1    Eveland, R.L.2    Gladwin, M.T.3    Swenson, E.R.4
  • 163
    • 0031415276 scopus 로고    scopus 로고
    • The hemoglobin system of Pleuragramma antarcticum – correlation of hematological and biochemical adaptations with lifestyle
    • M. Tamburrini R. D'Avino V. Carratore A. Kunzmann G. di Prisco The hemoglobin system of Pleuragramma antarcticum – correlation of hematological and biochemical adaptations with lifestyle Comp. Biochem. Physiol. 118A 1997 1037 1044
    • (1997) Comp. Biochem. Physiol. , vol.118A , pp. 1037-1044
    • Tamburrini, M.1    D'Avino, R.2    Carratore, V.3    Kunzmann, A.4    di Prisco, G.5
  • 165
    • 33646167802 scopus 로고    scopus 로고
    • Haemoconcentration via diuresis in short‐term hypoxia: Apossible role for cardiac natriuretic peptide in rainbow trout
    • V. Tervonen O. Vuolteenaho M. Nikinmaa Haemoconcentration via diuresis in short‐term hypoxia: Apossible role for cardiac natriuretic peptide in rainbow trout Comp. Biochem. Physiol. 144A 2006 86 92
    • (2006) Comp. Biochem. Physiol. , vol.144A , pp. 86-92
    • Tervonen, V.1    Vuolteenaho, O.2    Nikinmaa, M.3
  • 166
    • 0023463901 scopus 로고
    • Beta‐adrenergic control of blood oxygen affinity in acutely hypoxic exposed rainbow trout
    • V. Tetens N.J. Christensen Beta‐adrenergic control of blood oxygen affinity in acutely hypoxic exposed rainbow trout J. Comp. Physiol. 157B 1987 667 675
    • (1987) J. Comp. Physiol. , vol.157B , pp. 667-675
    • Tetens, V.1    Christensen, N.J.2
  • 167
    • 0006729488 scopus 로고
    • Antarctic fish blood: Respiratory properties and the effects of thermal acclimation
    • V. Tetens R.M.G. Wells A.L. DeVries Antarctic fish blood: Respiratory properties and the effects of thermal acclimation J. Exp. Biol. 109 1984 265 279
    • (1984) J. Exp. Biol. , vol.109 , pp. 265-279
    • Tetens, V.1    Wells, R.M.G.2    DeVries, A.L.3
  • 168
    • 13444270798 scopus 로고    scopus 로고
    • Behavioral and physiological compensation for chronic hypoxia in the sailfin molly (Poecilia latipinna)
    • C.M. Timmerman L.J. Chapman Behavioral and physiological compensation for chronic hypoxia in the sailfin molly ( Poecilia latipinna ) Physiol. Biochem. Zool. 77 2004 601 610
    • (2004) Physiol. Biochem. Zool. , vol.77 , pp. 601-610
    • Timmerman, C.M.1    Chapman, L.J.2
  • 169
    • 85120211586 scopus 로고    scopus 로고
    • Mutagenic studies on the origins of the Root effect
    • S. Unzai S‐Y. Park K. Nagai T. Brittain J.R.H. Tame Mutagenic studies on the origins of the Root effect M. Bolognesi G. Di Prisco C. Verde Dioxygen Binding and Sensing Proteins 2009 Springer‐Verlag Italy
    • (2009)
    • Unzai, S.1    Park, S‐Y.2    Nagai, K.3    Brittain, T.4    Tame, J.R.H.5
  • 170
    • 0034067349 scopus 로고    scopus 로고
    • Organic phosphates in the red blood cells of fish
    • A.L. Val Organic phosphates in the red blood cells of fish Comp. Biochem. Physiol. 125 2000 417 435
    • (2000) Comp. Biochem. Physiol. , vol.125 , pp. 417-435
    • Val, A.L.1
  • 173
    • 0022439308 scopus 로고
    • Hemoglobin heterogeneity and the oxygen affinity of the hemolysate of some Victorian cichlids
    • E. Verheyen R. Blust W. Decleir Hemoglobin heterogeneity and the oxygen affinity of the hemolysate of some Victorian cichlids Comp. Biochem. Physiol. 84A 1986 315 318
    • (1986) Comp. Biochem. Physiol. , vol.84A , pp. 315-318
    • Verheyen, E.1    Blust, R.2    Decleir, W.3
  • 174
    • 0002884437 scopus 로고
    • Functional significance and structural basis of multiple hemoglobins with special reference to ectothermic vertebrates
    • R.E. Weber Functional significance and structural basis of multiple hemoglobins with special reference to ectothermic vertebrates J.P. Truchot B. Lahlou Comparative Physiology; Animal Nutrition and Transport Processes, 2. Transport, Respiration and Excretion: Comparative and Environmental Aspects. II. Blood Oxygen Transport: Adjustment to Physiological and Environmental Conditions Vol. 6 1990 Karger Basel 58 75
    • (1990) , pp. 58-75
    • Weber, R.E.1
  • 175
    • 0041319615 scopus 로고    scopus 로고
    • Hemoglobin adaptations in Amazonian and temperate fish with special reference to hypoxia, allosteric effectors and functional heterogeneity
    • R.E. Weber Hemoglobin adaptations in Amazonian and temperate fish with special reference to hypoxia, allosteric effectors and functional heterogeneity A.L. Val V.M.F. Almeida‐Val D.J. Randall Physiology and Biochemistry of the Fishes of the Amazon 1996 INPA Brazil 75 90
    • (1996) , pp. 75-90
    • Weber, R.E.1
  • 176
    • 0011062010 scopus 로고    scopus 로고
    • Adaptations for oxygen transport: Lessons from fish hemoglobins
    • R.E. Weber Adaptations for oxygen transport: Lessons from fish hemoglobins G. Di Prisco B. Giardina R.E. Weber Hemoglobin Function in Vertebrates. Molecular Adaptation in Extreme and Temperate Environments 2000 Springer‐Verlag Italy 23 37
    • (2000) , pp. 23-37
    • Weber, R.E.1
  • 177
    • 0017187708 scopus 로고
    • Multiple haemoglobins in plaice and flounder and their functional properties
    • R.E. Weber J.A.M. de Wilde Multiple haemoglobins in plaice and flounder and their functional properties Comp. Biochem. Physiol. 54B 1976 433 437
    • (1976) Comp. Biochem. Physiol. , vol.54B , pp. 433-437
    • Weber, R.E.1    de Wilde, J.A.M.2
  • 178
    • 7944231804 scopus 로고    scopus 로고
    • Functional adaptation and its molecular basis in vertebrate hemoglobins, neuroglobins and cytoglobins
    • R.E. Weber A. Fago Functional adaptation and its molecular basis in vertebrate hemoglobins, neuroglobins and cytoglobins Resp. Physiol. Neurobiol. 144 2004 141 159
    • (2004) Resp. Physiol. Neurobiol. , vol.144 , pp. 141-159
    • Weber, R.E.1    Fago, A.2
  • 179
    • 0023866302 scopus 로고
    • Functional adaptations in hemoglobins from ectothermic vertebrates
    • R.E. Weber F.B. Jensen Functional adaptations in hemoglobins from ectothermic vertebrates Annu. Rev. Physiol. 50 1988 161 179
    • (1988) Annu. Rev. Physiol. , vol.50 , pp. 161-179
    • Weber, R.E.1    Jensen, F.B.2
  • 180
    • 1242277872 scopus 로고    scopus 로고
    • Novel” factors that regulate oxygen binding in vertebrate hemoglobins
    • R.E. Weber 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
  • 181
    • 0000602219 scopus 로고
    • Haemoglobin structure and function
    • R.E. Weber R.M.G. Wells Haemoglobin structure and function S.C. Wood Comparative Pulmonary Physiology 1989 Marcell Dekker New York 279 310
    • (1989) , pp. 279-310
    • Weber, R.E.1    Wells, R.M.G.2
  • 182
    • 0017014302 scopus 로고
    • Temperature acclimation and oxygen‐binding properties of blood and multiple haemoglobins from rainbow trout
    • R.E. Weber S.C. Wood J.P. Lomholt Temperature acclimation and oxygen‐binding properties of blood and multiple haemoglobins from rainbow trout J. Exp. Biol. 65 1976 333 345
    • (1976) J. Exp. Biol. , vol.65 , pp. 333-345
    • Weber, R.E.1    Wood, S.C.2    Lomholt, J.P.3
  • 183
    • 0017230736 scopus 로고
    • Physiological properties of eel haemoglobin: Hypoxic acclimation, phosphate effects and multiplicity
    • R.E. Weber G. Lykkeboe 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
  • 185
    • 0042928294 scopus 로고    scopus 로고
    • Hemoglobin function in deep‐sea and hydrothermal‐vent endemic fish: Symenchelis parasitica (Anguillidae) and Thermarces cerberus (Zoarcidae)
    • R.E. Weber S. Hourdez F. Knowles F. Lallier Hemoglobin function in deep‐sea and hydrothermal‐vent endemic fish: Symenchelis parasitica (Anguillidae) and Thermarces cerberus (Zoarcidae) J. Exp. Biol. 206 2003 2693 2702
    • (2003) J. Exp. Biol. , vol.206 , pp. 2693-2702
    • Weber, R.E.1    Hourdez, S.2    Knowles, F.3    Lallier, F.4
  • 186
    • 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 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. 287 2004 R454 R464
    • (2004) Am. J. Physiol. , vol.287 , pp. R454-R464
    • Weber, R.E.1    Voelter, W.2    Fago, A.3    Echner, H.4    Campanella, E.5    Low, P.S.6
  • 187
    • 0001280321 scopus 로고
    • Hemoglobin physiology in vertebrate animals: A cautionary approach to adaptationist thinking
    • R.M.G. Wells Hemoglobin physiology in vertebrate animals: A cautionary approach to adaptationist thinking R.G. Boutilier Advances in Comparative and Environmental Physiology 1990 Springer Heidelberg 143 161
    • (1990) , pp. 143-161
    • Wells, R.M.G.1
  • 188
    • 0033392020 scopus 로고    scopus 로고
    • Haemoglobin function in aquatic animals: Molecular adaptations to environmental challenge
    • R.M.G. Wells Haemoglobin function in aquatic animals: Molecular adaptations to environmental challenge Mar. Freshw. Res. 50 1999 933 939
    • (1999) Mar. Freshw. Res. , vol.50 , pp. 933-939
    • Wells, R.M.G.1
  • 189
    • 33748783925 scopus 로고    scopus 로고
    • Blood‐gas transport and haemoglobin function in polar fishes: Does low temperature explain physiological characters?
    • R.M.G. Wells Blood‐gas transport and haemoglobin function in polar fishes: Does low temperature explain physiological characters? J.F. Steffensen A.P. Farrell The Physiology of Polar Fishes W.S. Hoar D.R. Randall A.P. Farrell Fish Physiology Vol. 22 2005 Academic Press New York 281 316
    • (2005) , pp. 281-316
    • Wells, R.M.G.1
  • 190
    • 0001298793 scopus 로고
    • Oxygen transport potential in tropical reef fish with special reference to blood viscosity and haematocrit
    • R.M.G. Wells J. Baldwin Oxygen transport potential in tropical reef fish with special reference to blood viscosity and haematocrit J. Exp. Mar. Biol. Ecol. 141 1990 131 143
    • (1990) J. Exp. Mar. Biol. Ecol. , vol.141 , pp. 131-143
    • Wells, R.M.G.1    Baldwin, J.2
  • 191
    • 0025360589 scopus 로고
    • The spleen in hypoxic and exercised rainbow trout
    • R.M.G. Wells R.E. Weber The spleen in hypoxic and exercised rainbow trout J. Exp. Biol. 150 1990 461 466
    • (1990) J. Exp. Biol. , vol.150 , pp. 461-466
    • Wells, R.M.G.1    Weber, R.E.2
  • 192
    • 84985153817 scopus 로고
    • Comparative study of the erythrocytes and haemoglobins in nototheniid fishes from Antarctica
    • R.M.G. Wells M.D. Ashby S.J. Duncan J.A. Macdonald Comparative study of the erythrocytes and haemoglobins in nototheniid fishes from Antarctica J. Fish Biol. 17 1980 517 527
    • (1980) J. Fish Biol. , vol.17 , pp. 517-527
    • Wells, R.M.G.1    Ashby, M.D.2    Duncan, S.J.3    Macdonald, J.A.4
  • 193
    • 0022486025 scopus 로고
    • Physiological stress responses in big gamefish after capture: Observations on plasma chemistry and blood factors
    • R.M.G. Wells R.H. McIntyre A.K. Morgan P.S. Davie Physiological stress responses in big gamefish after capture: Observations on plasma chemistry and blood factors Comp. Biochem. Physiol. 84A 1986 565 571
    • (1986) Comp. Biochem. Physiol. , vol.84A , pp. 565-571
    • Wells, R.M.G.1    McIntyre, R.H.2    Morgan, A.K.3    Davie, P.S.4
  • 194
    • 34250088011 scopus 로고
    • Ecological and behavioural correlates of intracellular buffering capacity in the muscles of Antarctic fishes
    • R.M.G. Wells G. Summers L.A. Beard G.C. Grigg Ecological and behavioural correlates of intracellular buffering capacity in the muscles of Antarctic fishes Polar Biol. 8 1988 321 326
    • (1988) Polar Biol. , vol.8 , pp. 321-326
    • Wells, R.M.G.1    Summers, G.2    Beard, L.A.3    Grigg, G.C.4
  • 195
    • 0002419206 scopus 로고
    • Hypoxic responses in a fish from a stable environment: Blood oxygen transport in the Antarctic fish Pagothenia borchgrevinki
    • R.M.G. Wells G.C. Grigg L.A. Beard G. Summers Hypoxic responses in a fish from a stable environment: Blood oxygen transport in the Antarctic fish Pagothenia borchgrevinki J. Exp. Biol. 141 1989 97 111
    • (1989) J. Exp. Biol. , vol.141 , pp. 97-111
    • Wells, R.M.G.1    Grigg, G.C.2    Beard, L.A.3    Summers, G.4
  • 196
    • 0026086520 scopus 로고
    • The effect of β‐adrenergic stimulation of trout erythrocytes on blood viscosity
    • R.M.G. Wells P.S. Davie R.E. Weber The effect of β‐adrenergic stimulation of trout erythrocytes on blood viscosity Comp. Biochem. Physiol. 100C 1991 653 655
    • (1991) Comp. Biochem. Physiol. , vol.100C , pp. 653-655
    • Wells, R.M.G.1    Davie, P.S.2    Weber, R.E.3
  • 197
    • 0000561028 scopus 로고    scopus 로고
    • Blood oxygen transport and hemoglobin function in three tropical fish species from northern Australian freshwater billabongs
    • R.M.G. Wells J. Baldwin R.S. Seymour R.E. Weber Blood oxygen transport and hemoglobin function in three tropical fish species from northern Australian freshwater billabongs Fish Physiol. Biochem. 16 1997 247 258
    • (1997) Fish Physiol. Biochem. , vol.16 , pp. 247-258
    • Wells, R.M.G.1    Baldwin, J.2    Seymour, R.S.3    Weber, R.E.4
  • 199
    • 34249782838 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants and fish mitochondria
    • D. Wilhelm Filho Reactive oxygen species, antioxidants and fish mitochondria Frontiers in Bioscience 12 2007 1229 1237
    • (2007) Frontiers in Bioscience , vol.12 , pp. 1229-1237
    • Wilhelm Filho, D.1
  • 200
    • 34347404909 scopus 로고    scopus 로고
    • On optima: The case of myoglobin‐facilitated oxygen diffusion
    • J.B. Wittenberg On optima: The case of myoglobin‐facilitated oxygen diffusion Gene 398 2007 156 161
    • (2007) Gene , vol.398 , pp. 156-161
    • Wittenberg, J.B.1
  • 201
    • 0015527062 scopus 로고
    • Adaptation to hypoxia by increased HbO2 affinity and decreased red cell ATP concentration
    • 2 affinity and decreased red cell ATP concentration Nature, New Biol. 237 1972 278 279
    • (1972) Nature, New Biol. , vol.237 , pp. 278-279
    • Wood, S.C.1    Johansen, K.2
  • 202
    • 0018372623 scopus 로고
    • Respiratory properties of blood and hemoglobin solutions from the piranha
    • S.C. Wood R.E. Weber D.A. Powers Respiratory properties of blood and hemoglobin solutions from the piranha Comp. Biochem. Physiol. 62A 1979 163 167
    • (1979) Comp. Biochem. Physiol. , vol.62A , pp. 163-167
    • Wood, S.C.1    Weber, R.E.2    Powers, D.A.3
  • 203
    • 0036708698 scopus 로고    scopus 로고
    • Hypoxia: From molecular responses to ecosystem responses
    • R.S.S. Wu Hypoxia: From molecular responses to ecosystem responses Mar. Poll. Bull. 45 2002 35 45
    • (2002) Mar. Poll. Bull. , vol.45 , pp. 35-45
    • Wu, R.S.S.1
  • 204
    • 0001736917 scopus 로고
    • Respiratory, blood, and heart enzymatic adaptations of Sebastolobus alascanus (Scorpaenidae; Teleostei) to the oxygen minimum zone: A comparative study
    • T.‐H. Yang N.C. Lai G.N. Somero Respiratory, blood, and heart enzymatic adaptations of Sebastolobus alascanus (Scorpaenidae; Teleostei) to the oxygen minimum zone: A comparative study Biol. Bull. 183 1992 490 499
    • (1992) Biol. Bull. , vol.183 , pp. 490-499
    • Yang, T.‐H.1    Lai, N.C.2    Somero, G.N.3
  • 205
    • 33646500815 scopus 로고    scopus 로고
    • Neuropeptides and nitric oxide synthase in the gill and air‐breathing organs of fishes
    • G. Zaccone A. Mauceri S. Fasulo Neuropeptides and nitric oxide synthase in the gill and air‐breathing organs of fishes J. Exp. Zool. 305A 2006 428 439
    • (2006) J. Exp. Zool. , vol.305A , pp. 428-439
    • Zaccone, G.1    Mauceri, A.2    Fasulo, S.3


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