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Volumn 383, Issue 12, 2002, Pages 1907-1916

The primary structure of three hemoglabin chains from the indigo snake (Drymarchon corais erebunnus, separates): First evidence αD chains and two β chain types in snakes

Author keywords

Colubridae; Heme contract; Hemoglobin sequence

Indexed keywords

GLUTAMINE; HEMOGLOBIN A; HEMOGLOBIN CHAIN; HEMOGLOBIN D; HEMOGLOBIN VARIANT; HISTIDINE; UNCLASSIFIED DRUG; HEMOGLOBIN; PEPTIDE; TRYPSIN;

EID: 0038143162     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2002.214     Document Type: Review
Times cited : (6)

References (44)
  • 2
    • 0026196598 scopus 로고
    • Primary structure of hemoglobin from Monitor Lizard (Varanus exanthematicus albigularis - Squamata)
    • Abbasi, A., and Braunitzer, G. (1991). Primary structure of hemoglobin from Monitor Lizard (Varanus exanthematicus albigularis - Squamata). Biol. Chem. Hoppe-Seyler 372, 473-479.
    • (1991) Biol. Chem. Hoppe-Seyler , vol.372 , pp. 473-479
    • Abbasi, A.1    Braunitzer, G.2
  • 4
    • 0012274005 scopus 로고
    • Untersuchungen an Haemoglobinen der Bullennatter (Pituophis melanoleucus), Tigerpython (Python molurus bivittatus) und Indigonatter (Drymarchon corais erebennus)
    • Diploma Thesis, Universiy of Munich, Germany
    • Bittner, A. (1984). Untersuchungen an Haemoglobinen der Bullennatter (Pituophis melanoleucus), Tigerpython (Python molurus bivittatus) und Indigonatter (Drymarchon corais erebennus). Diploma Thesis, Universiy of Munich, Germany.
    • (1984)
    • Bittner, A.1
  • 5
    • 0028035278 scopus 로고
    • Interactions of adenosine triphosphate with snake hemoglobins. Studies in Liophis miliaris, Boa constrictor, and Bothrops alternatus
    • Bonilla, G.O., Oyama Jr., S., Nagatomo, C.L., Matsuura, M.S.A., and Focesi Jr., A. (1994). Interactions of adenosine triphosphate with snake hemoglobins. Studies in Liophis miliaris, Boa constrictor, and Bothrops alternatus. Comp. Biochem. Physiol. 109B, 701-707.
    • (1994) Comp. Biochem. Physiol. , vol.109 B , pp. 701-707
    • Bonilla, G.O.1    Oyama S., Jr.2    Nagatomo, C.L.3    Matsuura, M.S.A.4    Focesi A., Jr.5
  • 7
    • 0016227979 scopus 로고
    • Structural studies on chick embryonic hemoglobins
    • Brown, J.L., and Ingram, V.M. (1974). Structural studies on chick embryonic hemoglobins. J. Biol. Chem. 249, 3960-3972.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3960-3972
    • Brown, J.L.1    Ingram, V.M.2
  • 8
    • 0001797359 scopus 로고
    • Molecular systematics of neotropical xenodontine snakes. 1. South-American Xenodontines
    • Cadle, J.E. (1984). Molecular systematics of neotropical xenodontine snakes. 1. South-American Xenodontines. Herpetologica 40, 8-20.
    • (1984) Herpetologica , vol.40 , pp. 8-20
    • Cadle, J.E.1
  • 10
    • 0020069395 scopus 로고
    • Minor early embryonic chick hemoglobin M
    • Chapman, B.S., Hood, L.E., and Tobin, A.J. (1982). Minor early embryonic chick hemoglobin M. J. Biol. Chem. 257, 651-658.
    • (1982) J. Biol. Chem. , vol.257 , pp. 651-658
    • Chapman, B.S.1    Hood, L.E.2    Tobin, A.J.3
  • 11
    • 0019986337 scopus 로고
    • Phylogenetic origins and adaptive evolution of avian and mammalian hemoglobin genes
    • Czelusniak, J., Goodman, M., Hewett-Emmett, D., Weiss, M.L., Venta, P.J., and Tashian, R.E. (1982). Phylogenetic origins and adaptive evolution of avian and mammalian hemoglobin genes. Nature 298, 297-300.
    • (1982) Nature , vol.298 , pp. 297-300
    • Czelusniak, J.1    Goodman, M.2    Hewett-Emmett, D.3    Weiss, M.L.4    Venta, P.J.5    Tashian, R.E.6
  • 12
    • 0017929425 scopus 로고
    • A comparison of the electrophoretic haemoglobin patterns of the vertebrates
    • De Smet, W.H.O. (1978). A comparison of the electrophoretic haemoglobin patterns of the vertebrates. Acta Zool. Pathol. 70, 119-131.
    • (1978) Acta Zool. Pathol. , vol.70 , pp. 119-131
    • De Smet, W.H.O.1
  • 13
    • 0012332242 scopus 로고
    • Reptilian hemoglobins: N-terminal sequence of an α-chain of viper (Vipera aspis) hemoglobin
    • Duguet, M., Chauvet, J.P., and Acher, R. (1971). Reptilian hemoglobins: N-terminal sequence of an α-chain of viper (Vipera aspis) hemoglobin. FEBS Lett. 18, 185-188.
    • (1971) FEBS Lett. , vol.18 , pp. 185-188
    • Duguet, M.1    Chauvet, J.P.2    Acher, R.3
  • 14
    • 0016268872 scopus 로고
    • Phylogeny of hemoglobins: The complete amino acid sequence of an α-chain of viper (Vipera aspis) hemoglobin
    • Duguet, M., Chauvet, J.P., and Acher, R. (1974). Phylogeny of hemoglobins: the complete amino acid sequence of an α-chain of viper (Vipera aspis) hemoglobin. FEBS Lett. 47, 333-337.
    • (1974) FEBS Lett. , vol.47 , pp. 333-337
    • Duguet, M.1    Chauvet, J.P.2    Acher, R.3
  • 15
    • 0014064044 scopus 로고
    • A protein sequenator
    • Edman, P., and Begg. G. (1967). A protein sequenator. Eur. J. Biochem. 1, 80-91.
    • (1967) Eur. J. Biochem. , vol.1 , pp. 80-91
    • Edman, P.1    Begg, G.2
  • 17
    • 0021683974 scopus 로고
    • The crystal structure of human deoxyhaemoglobin at 1.4 Å resolution
    • Fermi, G., Perutz, M. F., Shaanan, B., and Fourme, R. (1984). The crystal structure of human deoxyhaemoglobin at 1.4 Å resolution. J. Mol. Biol. 175, 159-174.
    • (1984) J. Mol. Biol. , vol.175 , pp. 159-174
    • Fermi, G.1    Perutz, M.F.2    Shaanan, B.3    Fourme, R.4
  • 18
    • 0025236563 scopus 로고
    • Dimertetramer transition in hemoglobins from Liophis miliaris. II. Evidence with the stripped proteins
    • Focesi Jr., A., Ogo, S.H., and Matsuura, M.S.A. (1990). Dimertetramer transition in hemoglobins from Liophis miliaris. II. Evidence with the stripped proteins. Comp. Biochem. Physiol. 96B, 119-122.
    • (1990) Comp. Biochem. Physiol. , vol.96 B , pp. 119-122
    • Focesi A., Jr.1    Ogo, S.H.2    Matsuura, M.S.A.3
  • 19
    • 0026460919 scopus 로고
    • Dimer-tetramer transition in hemoglobin from Liophis miliaris. III. The phenomenon in snake species of different evolutionary levels
    • Focesi Jr., A., Bonilla, G.O., Nagatomo, C.L., and Matsuura, M.S.A. (1992). Dimer-tetramer transition in hemoglobin from Liophis miliaris. III. The phenomenon in snake species of different evolutionary levels. Comp. Biochem. Physiol. 103B, 985-989.
    • (1992) Comp. Biochem. Physiol. , vol.103 B , pp. 985-989
    • Focesi A., Jr.1    Bonilla, G.O.2    Nagatomo, C.L.3    Matsuura, M.S.A.4
  • 20
    • 0014939933 scopus 로고
    • The chromatographic determination of cystine and cysteine residues in proteins as S-β-(4-pyridylethyl)cysteine
    • Friedman, M., Krull, L.H., and Cavins, J.F. (1970). The chromatographic determination of cystine and cysteine residues in proteins as S-β-(4-pyridylethyl)cysteine. J. Biol. Chem. 245, 3868-3871.
    • (1970) J. Biol. Chem. , vol.245 , pp. 3868-3871
    • Friedman, M.1    Krull, L.H.2    Cavins, J.F.3
  • 21
    • 0029844788 scopus 로고    scopus 로고
    • The amino acid sequences of two α chains of hemoglobins from Komodo dragon Varanus komodoensis and phylogenetic relationships of amniotes
    • Fushitani K., Higashiyama K., Moriyama E.N., Imai K., and Hosokawa K. (1996). The amino acid sequences of two α chains of hemoglobins from Komodo dragon Varanus komodoensis and phylogenetic relationships of amniotes. Mol. Biol. Evol. 13, 1039-1043.
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 1039-1043
    • Fushitani, K.1    Higashiyama, K.2    Moriyama, E.N.3    Imai, K.4    Hosokawa, K.5
  • 22
    • 0000424154 scopus 로고
    • Molecular evolution above the species level - Branching pattern, rates, and mechanisms
    • Goodman, M., Weiss, M.L., and Czelusniak, J. (1982). Molecular evolution above the species level - branching pattern, rates, and mechanisms. Syst. Zool. 31, 376-399.
    • (1982) Syst. Zool. , vol.31 , pp. 376-399
    • Goodman, M.1    Weiss, M.L.2    Czelusniak, J.3
  • 23
    • 4243809181 scopus 로고
    • Haemoglobine: Sequenz und Phylogenie Die Primärstruktur von Globinketten des Quastenflossers (Latimeria chalumnae) sowie folgencler Reptilien: Galapagos-Meerechse (Amblyrhynchus cristatus), Grüner Leguan (Iguana iguana), Indigonatter (Drymarchon corais), Glattstirnkaiman (Paleosuchus palpebrosus)
    • Ph.D. Thesis, University of Munich, Germany
    • Gorr, T (1993). Haemoglobine: Sequenz und Phylogenie. Die Primärstruktur von Globinketten des Quastenflossers (Latimeria chalumnae) sowie folgencler Reptilien: Galapagos-Meerechse (Amblyrhynchus cristatus), Grüner Leguan (Iguana iguana), Indigonatter (Drymarchon corais), Glattstirnkaiman (Paleosuchus palpebrosus). Ph.D. Thesis, University of Munich, Germany.
    • (1993)
    • Gorr, T.1
  • 25
    • 0019877201 scopus 로고
    • A gas - Liquid solid phase peptide and protein sequenator
    • Hewick, R.M., Hunkapiller, M.W., Hood, L.E., and Dreyer, W.J. (1981). A gas - liquid solid phase peptide and protein sequenator. J. Biol. Chem. 256, 7990-7997.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7990-7997
    • Hewick, R.M.1    Hunkapiller, M.W.2    Hood, L.E.3    Dreyer, W.J.4
  • 26
    • 0023517601 scopus 로고
    • The primary structures of the major and minor hemoglobin-components of adult Andean goose (Chloephaga melanoptera, Anatidae): The mutation Leu→Ser in position 55 of the β-chain
    • Hiebl, I., Braunitzer, G., and Schneegans, D. (1987). The primary structures of the major and minor hemoglobin-components of adult Andean goose (Chloephaga melanoptera, Anatidae): the mutation Leu→Ser in position 55 of the β-chain. Biol. Chem. Hoppe-Seyler 368, 1559-1569.
    • (1987) Biol. Chem. Hoppe-Seyler , vol.368 , pp. 1559-1569
    • Hiebl, I.1    Braunitzer, G.2    Schneegans, D.3
  • 27
    • 0025604855 scopus 로고
    • Sea snake (Microcephalophis gracilis) hemoglobin: Primary structure and relationships to other forms
    • Islam, A., Persson, B., Zaidi, Z.H., and Joernvall, H. (1990). Sea snake (Microcephalophis gracilis) hemoglobin: Primary structure and relationships to other forms. J. Prot. Chem. 9, 533-541.
    • (1990) J. Prot. Chem. , vol.9 , pp. 533-541
    • Islam, A.1    Persson, B.2    Zaidi, Z.H.3    Joernvall, H.4
  • 29
    • 0019225434 scopus 로고
    • Identification of the phenylthiohydantoin derivatives of the amino acids by high pressure chromatography using a ternary, isocratic solvent system
    • Lottspeich, F. (1980). Identification of the phenylthiohydantoin derivatives of the amino acids by high pressure chromatography using a ternary, isocratic solvent system. Hoppe-Seyler's Z. Physiol. Chem. 361, 1829-1834.
    • (1980) Hoppe-Seyler's Z. Physiol. Chem. , vol.361 , pp. 1829-1834
    • Lottspeich, F.1
  • 30
    • 0023075899 scopus 로고
    • Dimertetramer transition in hemoglobin from Liophis miliaris. I. Effect of organic polyphosphates
    • Matsuura, M.S.A., Ogo, S.H., and Focesi Jr., A. (1987). Dimertetramer transition in hemoglobin from Liophis miliaris. I. Effect of organic polyphosphates. Comp. Biochem. Physiol. 86A, 683-687.
    • (1987) Comp. Biochem. Physiol. , vol.86 A , pp. 683-687
    • Matsuura, M.S.A.1    Ogo, S.H.2    Focesi A., Jr.3
  • 31
    • 0024961823 scopus 로고
    • The amino acid sequences of the α and β chains of hemoglobin from the snake, Liophis miliaris
    • Matsuura, M.S.A., Fushitani, K., and Riggs, A.F. (1989). The amino acid sequences of the α and β chains of hemoglobin from the snake, Liophis miliaris. J. Biol. Chem. 264, 5515-5521.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5515-5521
    • Matsuura, M.S.A.1    Fushitani, K.2    Riggs, A.F.3
  • 32
    • 24244447086 scopus 로고
    • Amino acid sequence of the β chain of hemoglobin from the snake Liophis miliaris
    • Matsuura, M.S.A., Focesi, A. Jr., Rosa, J.C., and Greene, L.J. (1992). Amino acid sequence of the β chain of hemoglobin from the snake Liophis miliaris. FASEB J. 6, A57.
    • (1992) FASEB J. , vol.6
    • Matsuura, M.S.A.1    Focesi A., Jr.2    Rosa, J.C.3    Greene, L.J.4
  • 33
    • 0012326652 scopus 로고
    • Snakes of the world
    • (London, UK: Blandford Press)
    • Mattison, C. (1986). Snakes of the world (London, UK: Blandford Press).
    • (1986)
    • Mattison, C.1
  • 35
    • 0023553084 scopus 로고
    • Partial sequence of hemoglobin from cobra (Naja naja naja)
    • Naqui, S., Nadvi, I.N., and Zaidi, Z.H. (1987). Partial sequence of hemoglobin from cobra (Naja naja naja). Biosci. Rep. 7, 813-819.
    • (1987) Biosci. Rep. , vol.7 , pp. 813-819
    • Naqui, S.1    Nadvi, I.N.2    Zaidi, Z.H.3
  • 36
    • 4243624462 scopus 로고
    • Hemoglobin βII chain - Indian cobra (Naja naja naja)
    • IPID ref. no. V0337
    • Naqui, S., Abbasi, A., and Zaidi, Z.H. (1991). Hemoglobin βII chain - Indian cobra (Naja naja naja). IPID, ref. no. V0337.
    • (1991)
    • Naqui, S.1    Abbasi, A.2    Zaidi, Z.H.3
  • 38
    • 0012278832 scopus 로고
    • Content of organic phosphates and their allosteric effects on hemoglobins from the water-snakes Helicops modestus and Liophis miliaris
    • Ogo, S.H., Matsuura, M.S.A., and Focesi Jr., A. (1984). Content of organic phosphates and their allosteric effects on hemoglobins from the water-snakes Helicops modestus and Liophis miliaris. Comp. Biochem. Physiol. 82A, 587-589.
    • (1984) Comp. Biochem. Physiol. , vol.82 A , pp. 587-589
    • Ogo, S.H.1    Matsuura, M.S.A.2    Focesi A., Jr.3
  • 39
    • 0027298770 scopus 로고
    • Bothrops alternatus hemoglobin components. Oxygen binding properties and globin chain hydrophobic analysis
    • Oyama, S. Jr., Nagatomo, C.L., Bonilla, G.O., Matsuura, M.S.A., and Focesi Jr., A. (1993). Bothrops alternatus hemoglobin components. Oxygen binding properties and globin chain hydrophobic analysis. Comp. Biochem. Physiol. 105B, 271-275.
    • (1993) Comp. Biochem. Physiol. , vol.105 B , pp. 271-275
    • Oyama S., Jr.1    Nagatomo, C.L.2    Bonilla, G.O.3    Matsuura, M.S.A.4    Focesi A., Jr.5
  • 40
    • 0018189174 scopus 로고
    • Resolution of hemoglobin subunits by electrophoresis in acid urea poly-acrylamid gels containning Triton X-100
    • Rovera, G., Magarian, C., and Borun, T.W. (1978). Resolution of hemoglobin subunits by electrophoresis in acid urea poly-acrylamid gels containning Triton X-100. Anal. Biochem. 85, 506-518.
    • (1978) Anal. Biochem. , vol.85 , pp. 506-518
    • Rovera, G.1    Magarian, C.2    Borun, T.W.3
  • 42
    • 0022377180 scopus 로고
    • High performance liquid chromatography separation of the globin chains of non human hemoglobins
    • Schroeder, W.A., Shelton, J.B., Shelton, J.R. Huynh, V., and Teplow, D.B. (1985). High performance liquid chromatography separation of the globin chains of non human hemoglobins. Hemoglobin 9, 461-482.
    • (1985) Hemoglobin , vol.9 , pp. 461-482
    • Schroeder, W.A.1    Shelton, J.B.2    Shelton, J.R.3    Huynh, V.4    Teplow, D.B.5
  • 43
    • 4243809180 scopus 로고
    • Hemoglobinas e haptoglobinas em serpentes
    • Ph.D. Thesis, Universidade Federal do Rio Grande do Sul, Brasil
    • Schwantes, A.R. (1972). Hemoglobinas e haptoglobinas em serpentes. Ph.D. Thesis, Universidade Federal do Rio Grande do Sul, Brasil.
    • (1972)
    • Schwantes, A.R.1
  • 44
    • 0012320854 scopus 로고
    • Sequenzermittlung von Schlangen-haemoglobinen. Primaerstruktur von Globinketten der Indigonatter (Drymarchon corais erebenus) und des Tigerpython (Pyhton molurus bivittatus)
    • Diploma Thesis, University of Munich, Germany
    • Stoeckelhuber, M. (1992). Sequenzermittlung von Schlangen-haemoglobinen. Primaerstruktur von Globinketten der Indigonatter (Drymarchon corais erebenus) und des Tigerpython (Pyhton molurus bivittatus). Diploma Thesis, University of Munich, Germany.
    • (1992)
    • Stoeckelhuber, M.1


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