메뉴 건너뛰기




Volumn 141, Issue 4, 2005, Pages 400-407

Two sites for GTP binding in cathodic haemoglobins from Anguilliformes

Author keywords

Anguilliformes; Bohr effect; Cathodic haemoglobin; Chloride; Fish; GTP; Oxygen affinity; Phosphate binding

Indexed keywords

CHLORIDE; GUANOSINE TRIPHOSPHATE; HEMOGLOBIN; ORGANOPHOSPHATE;

EID: 22144467640     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2005.04.013     Document Type: Article
Times cited : (7)

References (24)
  • 2
    • 0023079928 scopus 로고
    • Expression and genetics of caprine hemoglobins
    • M. Braend, L.L. Nesse, and G.D. Efremov Expression and genetics of caprine hemoglobins Anim. Genet. 18 1987 223 231
    • (1987) Anim. Genet. , vol.18 , pp. 223-231
    • Braend, M.1    Nesse, L.L.2    Efremov, G.D.3
  • 3
    • 0016416337 scopus 로고
    • Molecular adaptation to physiological requirements: The hemoglobin system of trout
    • B.L. Horecker E.R. Stadtman Academic Press New York
    • M. Brunori Molecular adaptation to physiological requirements: the hemoglobin system of trout B.L. Horecker E.R. Stadtman Current Topics in Cellular Regulation vol. 9 1975 Academic Press New York 1 39
    • (1975) Current Topics in Cellular Regulation , vol.9 , pp. 1-39
    • Brunori, M.1
  • 6
    • 0030037572 scopus 로고    scopus 로고
    • Oxygen equilibria of cathodic eel hemoglobin analysed in terms of the MWC model and Adair's successive oxygenation theory
    • R.J. Feuerlein, and R.E. Weber Oxygen equilibria of cathodic eel hemoglobin analysed in terms of the MWC model and Adair's successive oxygenation theory J. Comp. Physiol. B 165 1996 597 606
    • (1996) J. Comp. Physiol. B , vol.165 , pp. 597-606
    • Feuerlein, R.J.1    Weber, R.E.2
  • 7
    • 0019751816 scopus 로고
    • Measurement of binding of gaseous and non-gaseous ligands to hemoglobin by conventional spectrophotometric procedures
    • B. Giardina, and G. Amiconi Measurement of binding of gaseous and non-gaseous ligands to hemoglobin by conventional spectrophotometric procedures Methods Enzymol. 76 1981 417 427
    • (1981) Methods Enzymol. , vol.76 , pp. 417-427
    • Giardina, B.1    Amiconi, G.2
  • 9
    • 0023678447 scopus 로고
    • Hb G-Philadelphia, or [α68(E17)Asn → Lys], in North Sardinia: Detection by isoeletric focusing and HPLC of tryptic peptides
    • L. Manca, P. De Muro, and B. Masala Hb G-Philadelphia, or [α68(E17)Asn → Lys], in North Sardinia: detection by isoeletric focusing and HPLC of tryptic peptides Clin. Chim. Acta 177 1988 231 238
    • (1988) Clin. Chim. Acta , vol.177 , pp. 231-238
    • Manca, L.1    De Muro, P.2    Masala, B.3
  • 10
    • 0025760401 scopus 로고
    • Aγ(E19)Ile → Tyr] variant by isoelectric focusing in normal newborns and in adults affected by elevated fetal hemoglobin syndromes
    • Aγ(E19)Ile → Tyr] variant by isoelectric focusing in normal newborns and in adults affected by elevated fetal hemoglobin syndromes Clin. Chim. Acta 198 1991 195 202
    • (1991) Clin. Chim. Acta , vol.198 , pp. 195-202
    • Masala, B.1    Manca, L.2
  • 12
    • 0037591730 scopus 로고    scopus 로고
    • Structural-functional characterisation of the cathodic haemoglobin 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, and G. di Prisco Structural-functional characterisation of the cathodic haemoglobin 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
  • 13
    • 0025289366 scopus 로고
    • Influence of organic phosphates on the root effect of multiple fish hemoglobins
    • B. Pelster, and R.E. Weber Influence of organic phosphates on the root effect of multiple fish hemoglobins J. Exp. Biol. 149 1990 425 437
    • (1990) J. Exp. Biol. , vol.149 , pp. 425-437
    • Pelster, B.1    Weber, R.E.2
  • 14
    • 0015527286 scopus 로고
    • Hemoglobin adaptation for fast and slow water habitats in sympatric catostomid fishes
    • D.A. Powers Hemoglobin adaptation for fast and slow water habitats in sympatric catostomid fishes Science 177 1972 360 362
    • (1972) Science , vol.177 , pp. 360-362
    • Powers, D.A.1
  • 15
    • 0034805574 scopus 로고    scopus 로고
    • Molecular dynamics analysis of a second phosphate site in the hemoglobins of the seabird, south Polar skua. Is there a site-site migratory mechanism along the central cavity?
    • A. Riccio, M. Tamburrini, B. Giardina, and G. di Prisco Molecular dynamics analysis of a second phosphate site in the hemoglobins of the seabird, south Polar skua. Is there a site-site migratory mechanism along the central cavity? Biophys. J. 81 2001 1938 1946
    • (2001) Biophys. J. , vol.81 , pp. 1938-1946
    • Riccio, A.1    Tamburrini, M.2    Giardina, B.3    Di Prisco, G.4
  • 16
    • 0038163525 scopus 로고
    • Conservation of peculiar structural properties by the hemoglobins of anguilloid eels (Teleostei)
    • M. Rizzotti, S. Pagni, and F. Bentivegna Conservation of peculiar structural properties by the hemoglobins of anguilloid eels (Teleostei) Z. Zoolog. Syst. Evol.forsch. 28 1990 12 19
    • (1990) Z. Zoolog. Syst. Evol.forsch. , vol.28 , pp. 12-19
    • Rizzotti, M.1    Pagni, S.2    Bentivegna, F.3
  • 18
    • 0035055934 scopus 로고    scopus 로고
    • High-resolution crystal structure of deoxy hemoglobin complexed with a potent allosteric effector
    • M.K. Safo, C.M. Moure, J.C. Burnett, G.S. Joshi, and D.J. Abraham High-resolution crystal structure of deoxy hemoglobin complexed with a potent allosteric effector Protein Sci. 10 2001 951 957
    • (2001) Protein Sci. , vol.10 , pp. 951-957
    • Safo, M.K.1    Moure, C.M.2    Burnett, J.C.3    Joshi, G.S.4    Abraham, D.J.5
  • 19
    • 0033807219 scopus 로고    scopus 로고
    • Structural and functional analysis of the two hemoglobins of the Antarctic seabird Catharacta maccormicki
    • M. Tamburrini, A. Riccio, M. Romano, B. Giardina, and G. di Prisco Structural and functional analysis of the two hemoglobins of the Antarctic seabird Catharacta maccormicki Eur. J. Biochem. 267 2000 6089 6098
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6089-6098
    • Tamburrini, M.1    Riccio, A.2    Romano, M.3    Giardina, B.4    Di Prisco, G.5
  • 21
    • 0037184126 scopus 로고    scopus 로고
    • The functionally distinct hemoglobins of the Arctic spotted wolffish Anarhichas minor
    • C. Verde, V. Carratore, A. Riccio, M. Tamburrini, E. Parisi, and G. di Prisco The functionally distinct hemoglobins of the Arctic spotted wolffish Anarhichas minor J. Biol. Chem. 277 2002 36312 36320
    • (2002) J. Biol. Chem. , vol.277 , pp. 36312-36320
    • Verde, C.1    Carratore, V.2    Riccio, A.3    Tamburrini, M.4    Parisi, E.5    Di Prisco, G.6
  • 22
    • 0002884437 scopus 로고
    • Functional significance and structural basis of multiple hemoglobins with special reference to ectothermic vertebrates
    • J.P. Truchot B. Lahlou Animal Nutrition and Transport Processes Karger Basel
    • R.E. Weber Functional significance and structural basis of multiple hemoglobins with special reference to ectothermic vertebrates J.P. Truchot B. Lahlou Animal Nutrition and Transport Processes Transport, Respiration and Excretion: Comparative and Environmental Aspects vol. 6 1990 Karger Basel 58 75
    • (1990) Transport, Respiration and Excretion: Comparative and Environmental Aspects , vol.6 , pp. 58-75
    • Weber, R.E.1
  • 23
    • 0017230736 scopus 로고
    • Physiological properties of eel hemoglobin: Hypoxic acclimation, phosphate effects and multiplicity
    • R.E. Weber, G. Lykkeboe, and K. Johansen Physiological properties of eel hemoglobin: 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.