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Volumn 142, Issue 3, 2005, Pages 258-268

Axolotl hemoglobin: cDNA-derived amino acid sequences of two α globins and a β globin from an adult Ambystoma mexicanum

Author keywords

Ambystoma mexicanum; Amphibia; Axolotl; Evolution; Globin; Hemoglobin; Nucleotide sequence; Primary structure

Indexed keywords

ALPHA GLOBIN; BETA GLOBIN; COMPLEMENTARY DNA; HEMOGLOBIN;

EID: 26844491756     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2005.07.003     Document Type: Article
Times cited : (1)

References (57)
  • 2
    • 0014669953 scopus 로고
    • The hemoglobins of the bullfrog, Rana catesbeiana: I. Purification, amino acid composition, and oxygen equilibria
    • S. Aggarwal, and A. Riggs The hemoglobins of the bullfrog, Rana catesbeiana: I. Purification, amino acid composition, and oxygen equilibria J. Biol. Chem. 244 1969 2372 2383
    • (1969) J. Biol. Chem. , vol.244 , pp. 2372-2383
    • Aggarwal, S.1    Riggs, A.2
  • 3
    • 17944376871 scopus 로고
    • The haemoglobin of amphibia IX. Functional properties of haemoglobin from Ambystoma tigrinum tigrinum and Mexican axolotl
    • G. Amiconi, M. Brunori, E. Antonini, M. Sorcini, and L. Tentori The haemoglobin of amphibia IX. Functional properties of haemoglobin from Ambystoma tigrinum tigrinum and Mexican axolotl Int. J. Biochem. 1 1970 582 588
    • (1970) Int. J. Biochem. , vol.1 , pp. 582-588
    • Amiconi, G.1    Brunori, M.2    Antonini, E.3    Sorcini, M.4    Tentori, L.5
  • 5
    • 0016226922 scopus 로고
    • The hemoglobin of the bullfrog, Rana catesbeiana. Partial amino acid sequence of the β chain of the major adult component
    • T.O. Baldwin, and A. Riggs The hemoglobin of the bullfrog, Rana catesbeiana. Partial amino acid sequence of the β chain of the major adult component J. Biol. Chem. 249 1974 6110 6118
    • (1974) J. Biol. Chem. , vol.249 , pp. 6110-6118
    • Baldwin, T.O.1    Riggs, A.2
  • 6
    • 0022424143 scopus 로고
    • The pattern of expression of the Xenopus laevis tadpole (α-globin genes and the amino acid sequence of the three major tadpole α-globin polypeptides
    • D. Banville, and J.G. Williams The pattern of expression of the Xenopus laevis tadpole (α-globin genes and the amino acid sequence of the three major tadpole α-globin polypeptides Nucleic Acids Res. 13 1985 5407 5421
    • (1985) Nucleic Acids Res. , vol.13 , pp. 5407-5421
    • Banville, D.1    Williams, J.G.2
  • 7
    • 0018978924 scopus 로고
    • Hemoglobins of an amphibia, the neotenous Ambystoma mexicanum. Complete amino-acid sequence of the α chain of the major component using automatic solid-phase Edman degradation
    • J.-P. Boissel, H. Wajcman, and D. Labie Hemoglobins of an amphibia, the neotenous Ambystoma mexicanum. Complete amino-acid sequence of the α chain of the major component using automatic solid-phase Edman degradation Eur. J. Biochem. 103 1980 613 621
    • (1980) Eur. J. Biochem. , vol.103 , pp. 613-621
    • Boissel, J.-P.1    Wajcman, H.2    Labie, D.3
  • 9
    • 0019321646 scopus 로고
    • Complete amino acid sequences of the major early embryonic α-like globins of the chicken
    • B.S. Chapman, A.J. Tobin, and L.E. Hood Complete amino acid sequences of the major early embryonic α-like globins of the chicken J. Biol. Chem. 255 1980 9051 9059
    • (1980) J. Biol. Chem. , vol.255 , pp. 9051-9059
    • Chapman, B.S.1    Tobin, A.J.2    Hood, L.E.3
  • 10
    • 0015528209 scopus 로고
    • Phylogeny of hemoglobis. β chain of frog (Rana esculenta) hemoglobin
    • J.-P. Chauvet, and R. Acher Phylogeny of hemoglobis. β chain of frog (Rana esculenta) hemoglobin Biochemistry 11 1972 916 927
    • (1972) Biochemistry , vol.11 , pp. 916-927
    • Chauvet, J.-P.1    Acher, R.2
  • 12
    • 0000376430 scopus 로고
    • Erythrocyte differentiation during the metamorphic hemoglobin switch of Rana catesbeiana
    • A.R. Dorn, and R.H. Broyles Erythrocyte differentiation during the metamorphic hemoglobin switch of Rana catesbeiana Proc. Natl. Acad. Sci. U. S. A. 79 1982 5592 5596
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 5592-5596
    • Dorn, A.R.1    Broyles, R.H.2
  • 13
    • 0016186661 scopus 로고
    • The occurrence of biochemical metamorphic events without anatomical metamorphosis in the axolotl
    • T. Ducibella The occurrence of biochemical metamorphic events without anatomical metamorphosis in the axolotl Dev. Biol. 38 1974 175 186
    • (1974) Dev. Biol. , vol.38 , pp. 175-186
    • Ducibella, T.1
  • 14
    • 0014846334 scopus 로고
    • The hemoglobin of amphibia-X. Sedimentation behaviour of frog, triton and axolotl hemoglobins
    • R. Elli, A. Giuliani, L. Tentori, E. Chiancone, and E. Antonini The hemoglobin of amphibia-X. Sedimentation behaviour of frog, triton and axolotl hemoglobins Comp. Biochem. Physiol. 36 1970 163 171
    • (1970) Comp. Biochem. Physiol. , vol.36 , pp. 163-171
    • Elli, R.1    Giuliani, A.2    Tentori, L.3    Chiancone, E.4    Antonini, E.5
  • 15
    • 0016760252 scopus 로고
    • Three-dimensional Fourier synthesis of human deoxyhaemoglobin at 2.5 Å resolution: Refinement of the atomic model
    • G. Fermi Three-dimensional Fourier synthesis of human deoxyhaemoglobin at 2.5 Å resolution: refinement of the atomic model J. Mol. Biol. 97 1975 237 256
    • (1975) J. Mol. Biol. , vol.97 , pp. 237-256
    • Fermi, G.1
  • 16
    • 0014939933 scopus 로고
    • The chromatographic determination of cystine and cysteine residues in proteins as S-β-(4-pyridylethyl)cysteine
    • M. Friedman, L.H. Kruill, and J.F. Cavins The chromatographic determination of cystine and cysteine residues in proteins as S-β-(4-pyridylethyl)cysteine J. Biol. Chem. 245 1970 3868 3871
    • (1970) J. Biol. Chem. , vol.245 , pp. 3868-3871
    • Friedman, M.1    Kruill, L.H.2    Cavins, J.F.3
  • 17
    • 0024212067 scopus 로고
    • Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer
    • M.A. Frohman, M.K. Dush, and G.R. Martin Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer Proc. Natl. Acad. Sci. U. S. A. 85 1988 8998 9002
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 8998-9002
    • Frohman, M.A.1    Dush, M.K.2    Martin, G.R.3
  • 18
    • 0031720003 scopus 로고    scopus 로고
    • Phylogenetic analysis of reptilian hemoglobins: Trees, rates, and divergences
    • T.A. Gorr, B.K. Mable, and T. Kleinschmidt Phylogenetic analysis of reptilian hemoglobins: trees, rates, and divergences J. Mol. Evol. 47 1998 471 485
    • (1998) J. Mol. Evol. , vol.47 , pp. 471-485
    • Gorr, T.A.1    Mable, B.K.2    Kleinschmidt, T.3
  • 19
    • 0018359407 scopus 로고
    • Multiple hemoglobins in Triturus cristatus: Their degradation by sulfhydryl compounds
    • J.A. Grasso, G.P. Casale, and N.C. Chromey Multiple hemoglobins in Triturus cristatus: their degradation by sulfhydryl compounds Comp. Biochem. Physiol. B 63 1979 93 101
    • (1979) Comp. Biochem. Physiol. B , vol.63 , pp. 93-101
    • Grasso, J.A.1    Casale, G.P.2    Chromey, N.C.3
  • 21
    • 0015159749 scopus 로고
    • Developmental changes of erythropoiesis in cultured chick blastoderms
    • H.K. Hagopian, and V.M. Ingram Developmental changes of erythropoiesis in cultured chick blastoderms J. Cell Biol. 51 1971 440 451
    • (1971) J. Cell Biol. , vol.51 , pp. 440-451
    • Hagopian, H.K.1    Ingram, V.M.2
  • 22
    • 0013932662 scopus 로고
    • Biochemical metamorphosis of hemoglobin in Rana catesbeiana: III. Molecular change of hemoglobin during spontaneous metamorphosis
    • K. Hamada, Y. Sakai, K. Tsushima, and R. Shukuya Biochemical metamorphosis of hemoglobin in Rana catesbeiana: III. Molecular change of hemoglobin during spontaneous metamorphosis J. Biochem. 60 1966 37 41
    • (1966) J. Biochem. , vol.60 , pp. 37-41
    • Hamada, K.1    Sakai, Y.2    Tsushima, K.3    Shukuya, R.4
  • 23
    • 0015906685 scopus 로고
    • The oxygen affinity of axolotl blood and haemoglobin before and after metamorphosis
    • J. Hattingh, and H. Bartels The oxygen affinity of axolotl blood and haemoglobin before and after metamorphosis Respir. Physiol. 18 1973 1 13
    • (1973) Respir. Physiol. , vol.18 , pp. 1-13
    • Hattingh, J.1    Bartels, H.2
  • 24
    • 0018570714 scopus 로고
    • Analysis of Xenopus laevis globins during development and erythroid cell maturation and the construction of recombinant plasmids containing sequences derived from adult globin mRNA
    • C.C. Hentschel, R.M. Kay, and J.G. Williams Analysis of Xenopus laevis globins during development and erythroid cell maturation and the construction of recombinant plasmids containing sequences derived from adult globin mRNA Dev. Biol. 72 1979 350 363
    • (1979) Dev. Biol. , vol.72 , pp. 350-363
    • Hentschel, C.C.1    Kay, R.M.2    Williams, J.G.3
  • 25
    • 0020680868 scopus 로고
    • The Xenopus laevis globin gene family: Chromosomal arrangement and gene structure
    • H.A. Hosbach, T. Wyler, and R. Weber The Xenopus laevis globin gene family: chromosomal arrangement and gene structure Cell 32 1983 45 53
    • (1983) Cell , vol.32 , pp. 45-53
    • Hosbach, H.A.1    Wyler, T.2    Weber, R.3
  • 26
    • 0017138267 scopus 로고
    • Aquatic life at high altitude: Respiratory adaptations in the Lake Titicaca frog, Telmatobius culeus
    • V.H. Hutchison, H.B. Haines, and G. Engbretson Aquatic life at high altitude: respiratory adaptations in the Lake Titicaca frog, Telmatobius culeus Respir. Physiol. 27 1976 115 129
    • (1976) Respir. Physiol. , vol.27 , pp. 115-129
    • Hutchison, V.H.1    Haines, H.B.2    Engbretson, G.3
  • 27
    • 0031757669 scopus 로고    scopus 로고
    • Multiple sequence alignment with Clustal X
    • F. Jeanmougin, and J.D. Thompson Multiple sequence alignment with Clustal X Trends Biochem. Sci. 23 1998 403 405
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 403-405
    • Jeanmougin, F.1    Thompson, J.D.2
  • 28
    • 0018973068 scopus 로고
    • Linkage of adult α- And β-globin genes in X. laevis and gene duplication by tetraploidizaiton
    • A.J. Jeffreys, V. Wilson, D. Wood, and J.P. Simons Linkage of adult α- and β-globin genes in X. laevis and gene duplication by tetraploidizaiton Cell 21 1980 555 564
    • (1980) Cell , vol.21 , pp. 555-564
    • Jeffreys, A.J.1    Wilson, V.2    Wood, D.3    Simons, J.P.4
  • 29
    • 0021100643 scopus 로고
    • Complete nucleotide sequence of a cloned cDNA derived from the major adult α-globin mRNA of X. laevis
    • R.M. Kay, R. Harris, R.K. Patient, and J.G. Williams Complete nucleotide sequence of a cloned cDNA derived from the major adult α-globin mRNA of X. laevis Nucleic Acids Res. 11 1983 1537 1542
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1537-1542
    • Kay, R.M.1    Harris, R.2    Patient, R.K.3    Williams, J.G.4
  • 30
    • 0024227635 scopus 로고
    • The primary structures of the major and minor hemoglobin components of the great crested newt (Triturus cristatus, Urodela, Amphibia)
    • T. Kleinschmidt, J.G. Sgouros, and G. Braunitzer The primary structures of the major and minor hemoglobin components of the great crested newt (Triturus cristatus, Urodela, Amphibia) Biol. Chem. Hoppe-Seyler 369 1988 1343 1360
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 1343-1360
    • Kleinschmidt, T.1    Sgouros, J.G.2    Braunitzer, G.3
  • 31
    • 0022423676 scopus 로고
    • Comparative nucleotide sequence analysis of two types of larval β-globin mRNAs of Xenopus laevis
    • W. Knöchel, W. Meyerhof, J. Stalder, and R. Weber Comparative nucleotide sequence analysis of two types of larval β-globin mRNAs of Xenopus laevis Nucleic Acids Res. 13 1985 7899 7908
    • (1985) Nucleic Acids Res. , vol.13 , pp. 7899-7908
    • Knöchel, W.1    Meyerhof, W.2    Stalder, J.3    Weber, R.4
  • 32
    • 0022565012 scopus 로고
    • Multiple hemoglobins in Triturus cristatus: Their study by analytical isolelectrofocussing
    • S. Koussoulakos, G. Kaparos, and D. Stathakos Multiple hemoglobins in Triturus cristatus: their study by analytical isolelectrofocussing Comp. Biochem. Physiol. B 83 1986 475 481
    • (1986) Comp. Biochem. Physiol. B , vol.83 , pp. 475-481
    • Koussoulakos, S.1    Kaparos, G.2    Stathakos, D.3
  • 33
    • 0043205826 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction study of hemoglobin D from the Aldabra giant tortoise, Geochelone gigantea
    • T. Kuwada, T. Hasegawa, I. Satoh, K. Ishikawa, and F. Shishikura Crystallization and preliminary X-ray diffraction study of hemoglobin D from the Aldabra giant tortoise, Geochelone gigantea Prot. Peptide Letters 10 2003 422 425
    • (2003) Prot. Peptide Letters , vol.10 , pp. 422-425
    • Kuwada, T.1    Hasegawa, T.2    Satoh, I.3    Ishikawa, K.4    Shishikura, F.5
  • 34
    • 0015115074 scopus 로고
    • The haemoglobins of healthy and anemic Xenopus laevis
    • N. MacLean, and R.D. Jurd The haemoglobins of healthy and anemic Xenopus laevis J. Cell Sci. 9 1971 509 528
    • (1971) J. Cell Sci. , vol.9 , pp. 509-528
    • MacLean, N.1    Jurd, R.D.2
  • 35
    • 0020622533 scopus 로고
    • Embryonic and larval hemoglobins during the early development of the bullfrog, Rana catesbeiana
    • P.B. Maples, A.R. Dorn, and R.H. Broyles Embryonic and larval hemoglobins during the early development of the bullfrog, Rana catesbeiana Dev. Biol. 96 1983 515 519
    • (1983) Dev. Biol. , vol.96 , pp. 515-519
    • Maples, P.B.1    Dorn, A.R.2    Broyles, R.H.3
  • 36
    • 0024248002 scopus 로고
    • Determination of hemoglobin expression patterns in erythroid cells of Rana catesbeiana tadpoles
    • P.B. Maples, J.C. Palmer, and R.H. Broyles Determination of hemoglobin expression patterns in erythroid cells of Rana catesbeiana tadpoles Comp. Biochem. Physiol. B 91 1988 755 762
    • (1988) Comp. Biochem. Physiol. B , vol.91 , pp. 755-762
    • Maples, P.B.1    Palmer, J.C.2    Broyles, R.H.3
  • 37
    • 0019313853 scopus 로고
    • Hemoglobins of the tadpole of the bullfrog, Rana catesbeiana. Amino acid sequence of the α chain of a major component
    • T. Maruyama, K.W.K. Watt, and A. Riggs Hemoglobins of the tadpole of the bullfrog, Rana catesbeiana. Amino acid sequence of the α chain of a major component J. Biol. Chem. 255 1980 3285 3293
    • (1980) J. Biol. Chem. , vol.255 , pp. 3285-3293
    • Maruyama, T.1    Watt, K.W.K.2    Riggs, A.3
  • 38
    • 0002207181 scopus 로고
    • Hemoglobin function during the life history of the bullfrog
    • F.H. McCutcheon Hemoglobin function during the life history of the bullfrog J. Cell. Comp. Physiol. 8 1936 63 81
    • (1936) J. Cell. Comp. Physiol. , vol.8 , pp. 63-81
    • McCutcheon, F.H.1
  • 40
    • 0014432669 scopus 로고
    • Hemoglobin synthesis during amphibian metamorphosis: I. Chemical studies on the hemoglobins from larval and adult stages on Rana catesbeiana
    • B. Moss, and V.M. Ingram Hemoglobin synthesis during amphibian metamorphosis: I. Chemical studies on the hemoglobins from larval and adult stages on Rana catesbeiana J. Mol. Biol. 32 1968 481 492
    • (1968) J. Mol. Biol. , vol.32 , pp. 481-492
    • Moss, B.1    Ingram, V.M.2
  • 41
    • 0002723506 scopus 로고
    • Disorders of hemoglobin function and stability
    • R.I. Handin S.E. Lux T.P. Stossel J.B. Lippincott Co Philadelphia
    • R.L. Nagel Disorders of hemoglobin function and stability R.I. Handin S.E. Lux T.P. Stossel Blood: Principles and Practice of Hematology 1995 J.B. Lippincott Co Philadelphia 1591 1644
    • (1995) Blood: Principles and Practice of Hematology , pp. 1591-1644
    • Nagel, R.L.1
  • 42
    • 0016196073 scopus 로고
    • Three-dimensional structure of hemoglobin from the polychaete annelid Glycera dibranchiata, at 2.5 a resolution
    • E.A. Padlan, and W.E. Love Three-dimensional structure of hemoglobin from the polychaete annelid Glycera dibranchiata, at 2.5 A resolution J. Biol. Chem. 249 1974 4067 4078
    • (1974) J. Biol. Chem. , vol.249 , pp. 4067-4078
    • Padlan, E.A.1    Love, W.E.2
  • 43
    • 36949043245 scopus 로고
    • The Bohr effect and combination with organic phosphates
    • M.F. Perutz The Bohr effect and combination with organic phosphates Nature 228 1970 734 739
    • (1970) Nature , vol.228 , pp. 734-739
    • Perutz, M.F.1
  • 44
    • 0021004799 scopus 로고
    • Species adaptation in a protein molecule
    • M.F. Perutz Species adaptation in a protein molecule Mol. Biol. Evol. 1 1983 1 28
    • (1983) Mol. Biol. Evol. , vol.1 , pp. 1-28
    • Perutz, M.F.1
  • 45
    • 0014412965 scopus 로고
    • Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 Å resolution: The atomic model
    • M.F. Perutz, H. Muirhead, J.M. Cox, and L.C.G. Goaman Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 Å resolution: the atomic model Nature 219 1968 131 139
    • (1968) Nature , vol.219 , pp. 131-139
    • Perutz, M.F.1    Muirhead, H.2    Cox, J.M.3    Goaman, L.C.G.4
  • 46
    • 0023954146 scopus 로고
    • The primary structure of the major and minor hemoglobin component of adult Western painted turtle (Chrysemys picta bellii)
    • K.P. Rüchnagel, and G. Braunitzer The primary structure of the major and minor hemoglobin component of adult Western painted turtle (Chrysemys picta bellii) Biol. Chem. Hoppe-Seyler 369 1988 123 131
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 123-131
    • Rüchnagel, K.P.1    Braunitzer, G.2
  • 47
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • N. Saitou, and M. Nei The neighbor-joining method: a new method for reconstructing phylogenetic trees Mol. Biol. Evol. 4 1987 406 425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 48
    • 0036341905 scopus 로고    scopus 로고
    • The primary structure of hemoglobin D from the Aldabra giant tortoise, Geochelone gigantea
    • F. Shishikura The primary structure of hemoglobin D from the Aldabra giant tortoise, Geochelone gigantea Zool. Sci. 19 2002 197 206
    • (2002) Zool. Sci. , vol.19 , pp. 197-206
    • Shishikura, F.1
  • 49
    • 0023644671 scopus 로고
    • Amino acid sequence of the monomer subunit of the extracellular hemoglobin of Lumbricus terrestris
    • F. Shishikura, J.W. Snow, T. Gotoh, S.N. Vinogradov, and D.A. Walz Amino acid sequence of the monomer subunit of the extracellular hemoglobin of Lumbricus terrestris J. Biol. Chem. 262 1987 3123 3131
    • (1987) J. Biol. Chem. , vol.262 , pp. 3123-3131
    • Shishikura, F.1    Snow, J.W.2    Gotoh, T.3    Vinogradov, S.N.4    Walz, D.A.5
  • 50
    • 0035533435 scopus 로고    scopus 로고
    • The amino acid sequence of the α- And β-globin chains of hemoglobin from the Aldabra giant tortoises, Geochelone gigantea
    • F. Shishikura, and K. Takami The amino acid sequence of the α- and β-globin chains of hemoglobin from the Aldabra giant tortoises, Geochelone gigantea Zool. Sci. 18 2001 515 526
    • (2001) Zool. Sci. , vol.18 , pp. 515-526
    • Shishikura, F.1    Takami, K.2
  • 51
    • 0027724107 scopus 로고
    • The hemoglobin of the bullfrog, Rana catesbeiana. the cDNA-derived amino acid sequences of the α chains of adult hemoglobins B and C: Their roles in deoxygenation-induced aggregation
    • D.J. Smith, H. Zhu, P.R. Kolatkar, L.-T. Tam, T.O. Baldwin, B.A. Roe, R.H. Broyles, and A.F. Riggs The hemoglobin of the bullfrog, Rana catesbeiana. The cDNA-derived amino acid sequences of the α chains of adult hemoglobins B and C: their roles in deoxygenation-induced aggregation J. Biol. Chem. 268 1993 26961 26971
    • (1993) J. Biol. Chem. , vol.268 , pp. 26961-26971
    • Smith, D.J.1    Zhu, H.2    Kolatkar, P.R.3    Tam, L.-T.4    Baldwin, T.O.5    Roe, B.A.6    Broyles, R.H.7    Riggs, A.F.8
  • 52
    • 0022996603 scopus 로고
    • The hemoglobins of the bullfrog Rana catesbeiana. the structure of the β chain of component C and the role of the α chain in the formation of intermolecular disulfide bonds
    • L.-T. Tam, G.P. Gray, and A.F. Riggs The hemoglobins of the bullfrog Rana catesbeiana. The structure of the β chain of component C and the role of the α chain in the formation of intermolecular disulfide bonds J. Biol. Chem. 261 1986 8290 8294
    • (1986) J. Biol. Chem. , vol.261 , pp. 8290-8294
    • Tam, L.-T.1    Gray, G.P.2    Riggs, A.F.3
  • 54
    • 0019313853 scopus 로고
    • Hemoglobins of the tadpole of the bullfrog, Rana catesbeiana. Amino acid sequence of the β chain of a major component
    • K.W.K. Watt, T. Maruyama, and A. Riggs Hemoglobins of the tadpole of the bullfrog, Rana catesbeiana. Amino acid sequence of the β chain of a major component J. Biol. Chem. 255 1980 3294 3301
    • (1980) J. Biol. Chem. , vol.255 , pp. 3294-3301
    • Watt, K.W.K.1    Maruyama, T.2    Riggs, A.3
  • 55
    • 0025880745 scopus 로고
    • The switch from larval to adult globin gene expression in Xenopus laevis is mediated by erythoroid cells from distinct compartments
    • R. Weber, B. Blum, and P.R. Muller The switch from larval to adult globin gene expression in Xenopus laevis is mediated by erythoroid cells from distinct compartments Development 112 1991 1021 1029
    • (1991) Development , vol.112 , pp. 1021-1029
    • Weber, R.1    Blum, B.2    Muller, P.R.3
  • 57
    • 0034066898 scopus 로고    scopus 로고
    • Erythropoiesis and unexpected expression pattern of globin genes in the salamander Hynobius retradatus
    • M. Yamaguchi, H. Takahashi, and M. Wakahara Erythropoiesis and unexpected expression pattern of globin genes in the salamander Hynobius retradatus Dev. Genes Evol. 210 2000 180 189
    • (2000) Dev. Genes Evol. , vol.210 , pp. 180-189
    • Yamaguchi, M.1    Takahashi, H.2    Wakahara, M.3


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