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Volumn 206, Issue 15, 2003, Pages 2693-2702

Hemoglobin function in deep-sea and hydrothermal-vent endemic fish: Symenchelis parasitica (Anguillidae) and Thermarces cerberus (Zoarcidae)

Author keywords

Anguillid; Deep sea fish; Enthalpy; Hemoglobin; Hydrothermal vent; Oxygen binding; Symenchelis parasitica; Thermarces cerberus; Zoarcid

Indexed keywords

HEMOGLOBIN; OXYGEN;

EID: 0042928294     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: 10.1242/jeb.00475     Document Type: Article
Times cited : (16)

References (64)
  • 2
    • 0000692741 scopus 로고
    • The sulfide-binding protein in the blood of the vestimentiferan tube-worm, Riftia pachyptila, is the extracellular hemoglobin
    • Arp, A. J., Childress, J. J. and Vetter, R. D. (1987). The sulfide-binding protein in the blood of the vestimentiferan tube-worm, Riftia pachyptila, is the extracellular hemoglobin. J. Exp. Biol. 128, 139-158.
    • (1987) J. Exp. Biol. , vol.128 , pp. 139-158
    • Arp, A.J.1    Childress, J.J.2    Vetter, R.D.3
  • 3
    • 0025335350 scopus 로고
    • Oxygenation properties of the two co-occurring hemoglobins of the tube worm Riftia pachyptila
    • Arp, A. J., Doyle, M. L., Di Cera, E. and Gill, S. J. (1990). Oxygenation properties of the two co-occurring hemoglobins of the tube worm Riftia pachyptila. Respir. Physiol. 80, 323-334.
    • (1990) Respir. Physiol. , vol.80 , pp. 323-334
    • Arp, A.J.1    Doyle, M.L.2    Di Cera, E.3    Gill, S.J.4
  • 4
    • 0014985250 scopus 로고
    • Studies on the functional properties of fish hemoglobins. II. The oxygen equilibrium of the isolated hemoglobin components from trout blood
    • Binotti, I., Giovenco, S., Giardina, B., Antonini, E., Brunori, M. and Wyman, J. (1971). Studies on the functional properties of fish hemoglobins. II. The oxygen equilibrium of the isolated hemoglobin components from trout blood. Arch. Biochem. Biophys. 142, 274-280.
    • (1971) Arch. Biochem. Biophys. , vol.142 , pp. 274-280
    • Binotti, I.1    Giovenco, S.2    Giardina, B.3    Antonini, E.4    Brunori, M.5    Wyman, J.6
  • 5
    • 0017647788 scopus 로고
    • Effect of hydrostatic pressure on ligand binding to hemoglobin
    • Carey, F. G., Knowles, F. and Gibson, Q. H. (1977). Effect of hydrostatic pressure on ligand binding to hemoglobin. J. Biol. Chem. 252, 4102-4107.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4102-4107
    • Carey, F.G.1    Knowles, F.2    Gibson, Q.H.3
  • 6
    • 0001172639 scopus 로고
    • Pressure-temperature interactions on m4-lactate dehydrogenases from hydrothermal vent fishes - Evidence for adaptation to elevated-temperatures by the zoarcid Thermarces andersoni, but not by the bythitid, Bythites hollisi
    • Dahlhoff, E., Scheidemann, S. and Somero, G. (1990). Pressure-temperature interactions on m4-lactate dehydrogenases from hydrothermal vent fishes - evidence for adaptation to elevated-temperatures by the zoarcid Thermarces andersoni, but not by the bythitid, Bythites hollisi. Biol. Bull. 179, 134-139.
    • (1990) Biol. Bull. , vol.179 , pp. 134-139
    • Dahlhoff, E.1    Scheidemann, S.2    Somero, G.3
  • 8
    • 0030905324 scopus 로고    scopus 로고
    • The anodic hemoglobin of Anguilla anguilla. Molecular basis for allosteric effects in a Root-effect hemoglobin
    • Fago, A., Bendixen, E., Malte, H. and Weber, R. E. (1997b). The anodic hemoglobin of Anguilla anguilla. Molecular basis for allosteric effects in a Root-effect hemoglobin. J. Biol. Chem. 272, 15628-15635.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15628-15635
    • Fago, A.1    Bendixen, E.2    Malte, H.3    Weber, R.E.4
  • 9
    • 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
    • Fago, A., Carratore, V., Di Prisco, G., Feuerlein, R. J., Sottrup-Jensen, L. and Weber, R. E. (1995). 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, 18897-18902.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18897-18902
    • Fago, A.1    Carratore, V.2    Di Prisco, G.3    Feuerlein, R.J.4    Sottrup-Jensen, L.5    Weber, R.E.6
  • 10
    • 0031467184 scopus 로고    scopus 로고
    • Temperature-dependent enthalpy of oxygenation in Antarctic fish hemoglobins
    • Fago, A., Wells, R. M. G. and Weber, R. E. (1997a). Temperature-dependent enthalpy of oxygenation in Antarctic fish hemoglobins. Comp. Biochem. Physiol. B 118, 319-326.
    • (1997) Comp. Biochem. Physiol. B , vol.118 , pp. 319-326
    • Fago, A.1    Wells, R.M.G.2    Weber, R.E.3
  • 11
    • 0023656180 scopus 로고
    • Specifically carboxymethylated hemoglobin as an analogue of carbamino hemoglobin. Solution and X-ray studies of carboxymethylated hemoglobin and X-ray studies of carbamino hemoglobin
    • Fantl, W. J., Di Donato, A., Manning, J. M., Rogers, P. H. and Arnone, A. (1987). Specifically carboxymethylated hemoglobin as an analogue of carbamino hemoglobin. Solution and X-ray studies of carboxymethylated hemoglobin and X-ray studies of carbamino hemoglobin. J. Biol. Chem. 262, 12700-12713.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12700-12713
    • Fantl, W.J.1    Di Donato, A.2    Manning, J.M.3    Rogers, P.H.4    Arnone, A.5
  • 12
    • 0042321038 scopus 로고
    • Partial pressure of gases dissolved at great depth
    • Fenn, W. O. (1972). Partial pressure of gases dissolved at great depth. Science 176, 1011-1012.
    • (1972) Science , vol.176 , pp. 1011-1012
    • Fenn, W.O.1
  • 13
    • 0032445353 scopus 로고    scopus 로고
    • The haemoglobin system of the mudfish, Labeo capensis: Adaptations to temperature and hypoxia
    • Frey, B. J., Weber, R. E., Van Aardt, W. J. and Fago, A. (1998). The haemoglobin system of the mudfish, Labeo capensis: adaptations to temperature and hypoxia. Comp. Biochem. Physiol. B 120, 735-742.
    • (1998) Comp. Biochem. Physiol. B , vol.120 , pp. 735-742
    • Frey, B.J.1    Weber, R.E.2    Van Aardt, W.J.3    Fago, A.4
  • 14
    • 0028018837 scopus 로고
    • Chloride ion independence of the Bohr effect in a mutant human hemoglobin β (V1M+H2deleted)
    • Fronticelli, C., Pechik, I., Brinigar, W. S., Kowalczyk, J. and Gilliland, G. L. (1994). Chloride ion independence of the Bohr effect in a mutant human hemoglobin β (V1M+H2deleted). J. Biol. Chem. 269, 23965-23969.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23965-23969
    • Fronticelli, C.1    Pechik, I.2    Brinigar, W.S.3    Kowalczyk, J.4    Gilliland, G.L.5
  • 15
    • 0018377107 scopus 로고
    • Functional studies on the separated hemoglobin components of an air-breathing catfish, Hoplosternum littorate (Hancock)
    • Garlick, R. L., Bunn, H. F., Fyhn, H. J., Fyhn, U. E. H., Martin, J. P., Noble, R. W. and Powers, D. (1979). Functional studies on the separated hemoglobin components of an air-breathing catfish, Hoplosternum littorate (Hancock). Comp. Biochem. Physiol. A 62, 219-226.
    • (1979) Comp. Biochem. Physiol. A , vol.62 , pp. 219-226
    • Garlick, R.L.1    Bunn, H.F.2    Fyhn, H.J.3    Fyhn, U.E.H.4    Martin, J.P.5    Noble, R.W.6    Powers, D.7
  • 16
    • 0000887906 scopus 로고
    • Redesciption et étude de la biologie de Thermaces ceberus, poisson zoarcidae des zones hydrothermales actives de la dorsale du Pacifique oriental
    • Geistdoerfer, P. and Seuront, L. (1995). Redesciption et étude de la biologie de Thermaces ceberus, poisson zoarcidae des zones hydrothermales actives de la dorsale du Pacifique oriental. Cybium 19, 167-178.
    • (1995) Cybium , vol.19 , pp. 167-178
    • Geistdoerfer, P.1    Seuront, L.2
  • 18
    • 0015501732 scopus 로고
    • Structure and function of the hemoglobins of the carp, Cyprinus carpio
    • Gillen, R. G. and Riggs, A. (1972). Structure and function of the hemoglobins of the carp, Cyprinus carpio. J. Biol. Chem. 247, 6039-6046.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6039-6046
    • Gillen, R.G.1    Riggs, A.2
  • 19
    • 0015935317 scopus 로고
    • Structure and function of the isolated hemoglobins of the American eel, Anguilla rostrata
    • Gillen, R. G. and Riggs, A. (1973). Structure and function of the isolated hemoglobins of the American eel, Anguilla rostrata. J. Biol. Chem. 248, 1961-1969.
    • (1973) J. Biol. Chem. , vol.248 , pp. 1961-1969
    • Gillen, R.G.1    Riggs, A.2
  • 20
    • 0017652976 scopus 로고
    • The enhancement of the alkaline Bohr effect of some fish hemoglobins with adenosine triphosphate
    • Gillen, R. G. and Riggs, A. (1977). The enhancement of the alkaline Bohr effect of some fish hemoglobins with adenosine triphosphate. Arch. Biochem. Biophys. 183, 678-685.
    • (1977) Arch. Biochem. Biophys. , vol.183 , pp. 678-685
    • Gillen, R.G.1    Riggs, A.2
  • 21
    • 0021945157 scopus 로고
    • Hematology of three deep-sea fishes: A reflection of low metabolic rates
    • Graham, M. S., Haedrich, R. L. and Fletcher, G. L. (1985). Hematology of three deep-sea fishes: a reflection of low metabolic rates. Comp. Biochem. Physiol. A 80, 79-84.
    • (1985) Comp. Biochem. Physiol. A , vol.80 , pp. 79-84
    • Graham, M.S.1    Haedrich, R.L.2    Fletcher, G.L.3
  • 22
    • 0034180788 scopus 로고    scopus 로고
    • Gas transfer system in Alvinella pompejana (Annelida Polychaeta, Terebellida): Functional properties of intracellular and extracellular hemoglobins
    • Hourdez, S., Lallier, F. H., De Cian, M. C., Green, B. N., Weber, R. E. and Toulmond, A. (2000a). Gas transfer system in Alvinella pompejana (Annelida Polychaeta, Terebellida): functional properties of intracellular and extracellular hemoglobins. Physiol. Biochem. Zool. 73, 365-373.
    • (2000) Physiol. Biochem. Zool. , vol.73 , pp. 365-373
    • Hourdez, S.1    Lallier, F.H.2    De Cian, M.C.3    Green, B.N.4    Weber, R.E.5    Toulmond, A.6
  • 23
    • 0033105495 scopus 로고    scopus 로고
    • Characterization and functional properties of the extracellular coelomic hemoglobins from the deep-sea, hydrothermal vent scaleworm Branchipolynoe symmytilida
    • Hourdez, S., Lallier, F. H., Martin-Jézéquel, V., Weber, R. E., Toulmond, A. and Martin Jezequel, V. (1999). Characterization and functional properties of the extracellular coelomic hemoglobins from the deep-sea, hydrothermal vent scaleworm Branchipolynoe symmytilida. Proteins 34, 435-442.
    • (1999) Proteins , vol.34 , pp. 435-442
    • Hourdez, S.1    Lallier, F.H.2    Martin-Jézéquel, V.3    Weber, R.E.4    Toulmond, A.5    Martin Jezequel, V.6
  • 25
    • 0021104746 scopus 로고
    • Oxygen equilibrium studies on hemoglobin from the bluefin tuna (Thunnus thynnus)
    • Ikeda-Saito, M., Yonetani, T. and 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
  • 27
    • 0022704194 scopus 로고
    • 2 saturation on red cell pH in tench blood in vivo and in vitro
    • 2 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
  • 28
    • 0032190855 scopus 로고    scopus 로고
    • Interaction between haemoglobin and synthetic peptides of the N-terminal cytoplasmic fragment of trout band 3 (AE1) protein
    • Jensen, F. B., Jakobsen, M. H. and Weber, R. E. (1998). Interaction between haemoglobin and synthetic peptides of the N-terminal cytoplasmic fragment of trout band 3 (AE1) protein. J. Exp. Biol. 201, 2685-2690.
    • (1998) J. Exp. Biol. , vol.201 , pp. 2685-2690
    • Jensen, F.B.1    Jakobsen, M.H.2    Weber, R.E.3
  • 29
    • 0005135196 scopus 로고
    • Oxygen-carrying proteins: A comparison of the oxygenation reaction in hemocyanin and hemerythrin with that in hemoglobin
    • Klotz, I. M. and Klotz, T. A. (1955). Oxygen-carrying proteins: a comparison of the oxygenation reaction in hemocyanin and hemerythrin with that in hemoglobin. Science 121, 477-480.
    • (1955) Science , vol.121 , pp. 477-480
    • Klotz, I.M.1    Klotz, T.A.2
  • 31
    • 0027009339 scopus 로고    scopus 로고
    • Hydrothermal discharge and alteration in near-surface sediments from the Guaymas basin, Gulf of California
    • Magemheim, A. J. and Gieskes, J. M. (2002). Hydrothermal discharge and alteration in near-surface sediments from the Guaymas basin, Gulf of California. Geochim. Cosmochim. Acta 56, 2329-2338.
    • (2002) Geochim. Cosmochim. Acta , vol.56 , pp. 2329-2338
    • Magemheim, A.J.1    Gieskes, J.M.2
  • 34
    • 0023055084 scopus 로고
    • Functional properties of hemoglobins from deep-sea fish: Correlations with depth distribution and presence of a swimbladder
    • Noble, R. W., Kwiatkowski, L. D., De Young, A., Davis, B. J., Haedrich, R. L., Tam, L.-T. and Riggs, A. F. (1986). Functional properties of hemoglobins from deep-sea fish: correlations with depth distribution and presence of a swimbladder. Biochim. Biophys. Acta 870, 552-563.
    • (1986) Biochim. Biophys. Acta , vol.870 , pp. 552-563
    • Noble, R.W.1    Kwiatkowski, L.D.2    De Young, A.3    Davis, B.J.4    Haedrich, R.L.5    Tam, L.-T.6    Riggs, A.F.7
  • 35
    • 0016717943 scopus 로고
    • Studies of the functional properties of the hemoglobin from the benthic fish, Antimora rostrata
    • Noble, R. W., Pennelly, R. R. and Riggs, A. (1975). Studies of the functional properties of the hemoglobin from the benthic fish, Antimora rostrata. Comp. Biochem. Physiol. B 52, 75-81.
    • (1975) Comp. Biochem. Physiol. B , vol.52 , pp. 75-81
    • Noble, R.W.1    Pennelly, R.R.2    Riggs, A.3
  • 38
    • 0028245286 scopus 로고
    • The chloride effect in human haemoglobin. A new kind of allosteric mechanism
    • Perutz, M. F., Shih, D. T. and Williamson, D. (1994). The chloride effect in human haemoglobin. A new kind of allosteric mechanism. J. Mol. Biol. 239, 555-560.
    • (1994) J. Mol. Biol. , vol.239 , pp. 555-560
    • Perutz, M.F.1    Shih, D.T.2    Williamson, D.3
  • 39
    • 0015527286 scopus 로고
    • Hemoglobin adaptation for fast and slow water habitats in sympatric catostomid fishes
    • Powers, D. A. (1972). Hemoglobin adaptation for fast and slow water habitats in sympatric catostomid fishes. Science 177, 360-362.
    • (1972) Science , vol.177 , pp. 360-362
    • Powers, D.A.1
  • 40
    • 0015523820 scopus 로고
    • Multiple hemoglobins of catostomid fish. I. Isolation and characterization of the isohemoglobins from Catostomus clarkii
    • Powers, D. A. and Edmundson, A. B. (1972). Multiple hemoglobins of catostomid fish. I. Isolation and characterization of the isohemoglobins from Catostomus clarkii. J. Biol. Chem. 247, 6686-6693.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6686-6693
    • Powers, D.A.1    Edmundson, A.B.2
  • 41
    • 0022503739 scopus 로고
    • Pressure increases oxygen affinity of whole blood and erythrocyte suspensions
    • Reeves, R. B. and Morin, R. A. (1986). Pressure increases oxygen affinity of whole blood and erythrocyte suspensions. J. Appl. Physiol. 61, 486-494.
    • (1986) J. Appl. Physiol. , vol.61 , pp. 486-494
    • Reeves, R.B.1    Morin, R.A.2
  • 42
    • 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
  • 43
    • 0036187568 scopus 로고    scopus 로고
    • Fish at high pressure: A hundred year history
    • Sebert, P. (2002). Fish at high pressure: a hundred year history. Comp. Biochem. Physiol. A 131, 575-585.
    • (2002) Comp. Biochem. Physiol. A , vol.131 , pp. 575-585
    • Sebert, P.1
  • 45
    • 0001418696 scopus 로고
    • Hemoglobin from the "Pompeii Worm", Alvinella pompejana, an annelid from a deep sea hot hydrothermal vent environment
    • Terwilliger, N. B. and Terwilliger, R. C. (1984). Hemoglobin from the "Pompeii Worm", Alvinella pompejana, an annelid from a deep sea hot hydrothermal vent environment. Mar. Biol. Lett. 5, 191-201.
    • (1984) Mar. Biol. Lett. , vol.5 , pp. 191-201
    • Terwilliger, N.B.1    Terwilliger, R.C.2
  • 46
    • 0000288364 scopus 로고
    • Extracellular hemoglobins of hydrothermal vent annelids: Structural and functional characteristics in three Alvinellid species
    • Toulmond, A., Slitine, F. E. I., De Frescheville, J. and Jouin, C. (1990). Extracellular hemoglobins of hydrothermal vent annelids: structural and functional characteristics in three Alvinellid species. Biol. Bull. 179, 366-373.
    • (1990) Biol. Bull. , vol.179 , pp. 366-373
    • Toulmond, A.1    Slitine, F.E.I.2    De Frescheville, J.3    Jouin, C.4
  • 47
    • 0025665773 scopus 로고
    • Seafloor hydrothermal activity: Black smocker chemistry and chimneys
    • Von Damm, K. L. (1990). Seafloor hydrothermal activity: black smocker chemistry and chimneys. Annu. Rev. Earth. Planet. Sci. 18, 173-204.
    • (1990) Annu. Rev. Earth. Planet. Sci. , vol.18 , pp. 173-204
    • Von Damm, K.L.1
  • 48
    • 85010901677 scopus 로고
    • Controls on the chemistry and temporal variability of seafloor hydrothermal fluids
    • ed. S. E. Humphris, R. A. Zierenberg, L. S. Mullineaux and R. E. Thompson. Washington, DC: American Geophysical Union
    • Von Damm, K. L. (1995). Controls on the chemistry and temporal variability of seafloor hydrothermal fluids. In Seafloor Hydrothermal Systems. Physical, Chemical, Biological, and Geological Interactions (ed. S. E. Humphris, R. A. Zierenberg, L. S. Mullineaux and R. E. Thompson), pp. 222-247. Washington, DC: American Geophysical Union.
    • (1995) Seafloor Hydrothermal Systems. Physical, Chemical, Biological, and Geological Interactions , pp. 222-247
    • Von Damm, K.L.1
  • 50
    • 0019413477 scopus 로고
    • 2 affinity in lugworm erythrocruorin
    • 2 affinity in lugworm erythrocruorin. Nature 292, 386-387.
    • (1981) Nature , vol.292 , pp. 386-387
    • Weber, R.E.1
  • 52
    • 0026602895 scopus 로고
    • Use of ionic and zwitterionic (Tris/BisTris and HEPES) buffers in studies on hemoglobin function
    • Weber, R. E. (1992). Use of ionic and zwitterionic (Tris/BisTris and HEPES) buffers in studies on hemoglobin function. J. Appl. Physiol. 72, 1611-1615.
    • (1992) J. Appl. Physiol. , vol.72 , pp. 1611-1615
    • Weber, R.E.1
  • 53
    • 0041319615 scopus 로고    scopus 로고
    • Hemoglobin adaptations in Amazonian and temperate fish with special reference to hypoxia, allosteric effectors and functional heterogeneity
    • ed. A. L. Val, V. M. F. Almeida-Val and D. J. Randall. Brazil: INPA
    • Weber, R. E. (1996). Hemoglobin adaptations in Amazonian and temperate fish with special reference to hypoxia, allosteric effectors and functional heterogeneity. In Physiology and Biochemistry of the Fishes of the Amazon (ed. A. L. Val, V. M. F. Almeida-Val and D. J. Randall), pp. 75-90. Brazil: INPA.
    • (1996) Physiology and Biochemistry of the Fishes of the Amazon , pp. 75-90
    • Weber, R.E.1
  • 54
    • 0011062010 scopus 로고    scopus 로고
    • Adaptations for oxygen transport: Lessons from fish hemoglobins
    • ed. G. Di Prisco, B. Giardina and R. E. Weber. Milan: Springer-Verlag Italia
    • Weber, R. E. (2000a). Adaptations for oxygen transport: Lessons from fish hemoglobins. In Hemoglobin Function in Vertebrates, Molecular Adaptation in Extreme and Temperate Environments (ed. G. Di Prisco, B. Giardina and R. E. Weber), pp. 23-37. Milan: Springer-Verlag Italia.
    • (2000) Hemoglobin Function in Vertebrates, Molecular Adaptation in Extreme and Temperate Environments , pp. 23-37
    • Weber, R.E.1
  • 55
    • 24244457372 scopus 로고    scopus 로고
    • Molecular adaptations in haemoglobin function: Intracellular effectors and red cell membrane interaction
    • Weber, R. E. (2000b). Molecular adaptations in haemoglobin function: intracellular effectors and red cell membrane interaction. Comp. Biochem. Physiol. B 126, S102.
    • (2000) Comp. Biochem. Physiol. B , vol.126
    • Weber, R.E.1
  • 56
    • 0034625456 scopus 로고    scopus 로고
    • Isohemoglobin differentiation in the bimodal-breathing Amazon catfish Hoplosternum littorale
    • Weber, R. E., Fago A., Val, A. L., Bang, A., Van Hauwaert, M. L., Dewilde, S., Zal, F. and Moens, L. (2000). Isohemoglobin differentiation in the bimodal-breathing Amazon catfish Hoplosternum littorale. J. Biol. Chem. 275, 17297-17305.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17297-17305
    • Weber, R.E.1    Fago, A.2    Val, A.L.3    Bang, A.4    Van Hauwaert, M.L.5    Dewilde, S.6    Zal, F.7    Moens, L.8
  • 57
    • 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. and Cox, R. P. (1987). 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. B 157, 145-152.
    • (1987) J. Comp. Physiol. B , vol.157 , pp. 145-152
    • Weber, R.E.1    Jensen, F.B.2    Cox, R.P.3
  • 58
    • 0017230736 scopus 로고
    • Physiological properties of eel haemoglobin: Hypoxic acclimation, phosphate effects and multiplicity
    • Weber, R. E., Lykkeboe, G. and Johansen, K. (1976a). Physiological properties of eel haemoglobin: Hypoxic acclimation, phosphate effects and multiplicity. J. Exp. Biol. 64, 75-88.
    • (1976) J. Exp. Biol. , vol.64 , pp. 75-88
    • Weber, R.E.1    Lykkeboe, G.2    Johansen, K.3
  • 59
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • Weber, R. E. and 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
  • 61
    • 0018408760 scopus 로고
    • Effects of erythrocytic nucleoside triphosphates on oxygen equilibria of composite and fractionated hemoglobins from the facultative air-breathing Amazonian catfish, Hypostomus and Pterygoplichthys
    • Weber, R. E. and Wood, S. C. (1979). Effects of erythrocytic nucleoside triphosphates on oxygen equilibria of composite and fractionated hemoglobins from the facultative air-breathing Amazonian catfish, Hypostomus and Pterygoplichthys. Comp. Biochem. Physiol. A 62, 179-183.
    • (1979) Comp. Biochem. Physiol. A , vol.62 , pp. 179-183
    • Weber, R.E.1    Wood, S.C.2
  • 62
    • 0017014302 scopus 로고
    • Temperature acclimation and oxygen-binding properties of blood and multiple haemoglobins of rainbow trout
    • Weber, E., Wood, S. C. and Lomholt, J. P. (1976b). Temperature acclimation and oxygen-binding properties of blood and multiple haemoglobins of rainbow trout. J. Exp. Biol. 65, 333-345.
    • (1976) J. Exp. Biol. , vol.65 , pp. 333-345
    • Weber, E.1    Wood, S.C.2    Lomholt, J.P.3
  • 63
    • 0017337229 scopus 로고
    • The balance sheet of a hemoglobin. Thermodynamics of CO binding by hemoglobin Trout I
    • Wyman, J., Gill, S. J., Noll, L., Giardina, B., Colosimo, A. and Brunori, M. (1977). The balance sheet of a hemoglobin. Thermodynamics of CO binding by hemoglobin Trout I. J. Mol. Biol. 109, 195-205.
    • (1977) J. Mol. Biol. , vol.109 , pp. 195-205
    • Wyman, J.1    Gill, S.J.2    Noll, L.3    Giardina, B.4    Colosimo, A.5    Brunori, M.6
  • 64
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • Wyman, J., Jr (1964). Linked functions and reciprocal effects in hemoglobin: a second look. Adv. Prot. Chem. 19, 223-286.
    • (1964) Adv. Prot. Chem. , vol.19 , pp. 223-286
    • Wyman J., Jr.1


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