메뉴 건너뛰기




Volumn 68, Issue 1, 2004, Pages 159-169

The primary structure of a novel goose-type lysozyme from rhea egg white

Author keywords

Amino acid sequence; G type lysozyme; Lysozyme; Rhea

Indexed keywords

AMINO ACID; CHITINASE; EGG PROTEIN; LYSOZYME; VEGETABLE PROTEIN;

EID: 4544348304     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.68.159     Document Type: Article
Times cited : (23)

References (53)
  • 1
    • 0000385093 scopus 로고
    • The amino acid sequence of egg white lysozyme
    • Canfield, R. E., The amino acid sequence of egg white lysozyme. J. Biol. Chem., 238, 2698-2707 (1963).
    • (1963) J. Biol. Chem. , vol.238 , pp. 2698-2707
    • Canfield, R.E.1
  • 2
    • 0000676684 scopus 로고
    • La structure chimique du lysozyme de blanc d'oeuf de poule: Etude detailee
    • Jollès, J., Jauregui-Adell, J., Bernier, I., and Jollès, P., La structure chimique du lysozyme de blanc d'oeuf de poule: etude detailee. Biochim. Biophys. Acta, 78, 668-689 (1963).
    • (1963) Biochim. Biophys. Acta , vol.78 , pp. 668-689
    • Jollès, J.1    Jauregui-Adell, J.2    Bernier, I.3    Jollès, P.4
  • 3
    • 0013852463 scopus 로고
    • Structure of hen egg white lysozyme. A three-dimensional Fourier synthesis at 2 Å resolution
    • Blake, C. C. F., Koenig, D. F., Mair, G. A., North, A. C. T., Phillips, D. C., and Serma, V. R., Structure of hen egg white lysozyme. A three-dimensional Fourier synthesis at 2 Å resolution. Nature, 206, 757-761 (1965).
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.F.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.T.4    Phillips, D.C.5    Serma, V.R.6
  • 4
    • 0014962420 scopus 로고
    • The amino acid sequence of T4 phage lysozyme. IV. Diluted acid hydrolysis and order of tryptic peptides
    • Inoye, M., Imada, M., and Tsugita, A., The amino acid sequence of T4 phage lysozyme. IV. Diluted acid hydrolysis and order of tryptic peptides. J. Biol. Chem., 245, 3479-3484 (1970).
    • (1970) J. Biol. Chem. , vol.245 , pp. 3479-3484
    • Inoye, M.1    Imada, M.2    Tsugita, A.3
  • 5
    • 0346436100 scopus 로고
    • The three-dimensional structure of the lysozyme from bacteriophage T4
    • Matthews, B. W., and Remington, S. J., The three-dimensional structure of the lysozyme from bacteriophage T4. Proc. Natl. Acad. Sci. USA, 71, 4178-4182 (1974).
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4178-4182
    • Matthews, B.W.1    Remington, S.J.2
  • 6
    • 0001470610 scopus 로고
    • Complete amino acid sequence of embden goose (Anwer anwer) egg-white lysozyme
    • Simpson, R. J., and Morgan, F. J., Complete amino acid sequence of embden goose (Anwer anwer) egg-white lysozyme. Biochim. Biophys. Acta, 744, 349-351 (1983).
    • (1983) Biochim. Biophys. Acta , vol.744 , pp. 349-351
    • Simpson, R.J.1    Morgan, F.J.2
  • 7
    • 0020629394 scopus 로고
    • Goose lysozyme structure: An evolutionary link between hen and bacteriophage lysozyme?
    • Grütter, M. G., Weaver, L. H., and Matthews, B. W., Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozyme? Nature, 303, 828-831 (1983).
    • (1983) Nature , vol.303 , pp. 828-831
    • Grütter, M.G.1    Weaver, L.H.2    Matthews, B.W.3
  • 8
    • 0021783520 scopus 로고
    • Three-dimensional structure of goose-type lysozyme from the egg white of the Australian black swan, Cygnus atratus
    • Isaacs, N. W., Machin, K. J., and Masakuni, M., Three-dimensional structure of goose-type lysozyme from the egg white of the Australian black swan, Cygnus atratus. Aust. J. Biol. Sci., 38, 13-22 (1985).
    • (1985) Aust. J. Biol. Sci. , vol.38 , pp. 13-22
    • Isaacs, N.W.1    Machin, K.J.2    Masakuni, M.3
  • 9
    • 0015500904 scopus 로고
    • Amino acid sequence studies on bobwhite quail egg white lysozyme
    • Prager, E. M., Arnheim, N., Mross, G. A., and Wilson, A. C., Amino acid sequence studies on bobwhite quail egg white lysozyme. J. Biol. Chem., 247, 2905-2916 (1972).
    • (1972) J. Biol. Chem. , vol.247 , pp. 2905-2916
    • Prager, E.M.1    Arnheim, N.2    Mross, G.A.3    Wilson, A.C.4
  • 10
    • 0025490494 scopus 로고
    • The amino acid sequence of Lady Amherest's pheasant (Chrysolophus amherstiae) and golden pheasant (Chrysolophus pictus) egg-white lysozymes
    • Araki, T., Kuramoto, M., and Torikata, T., The amino acid sequence of Lady Amherest's pheasant (Chrysolophus amherstiae) and golden pheasant (Chrysolophus pictus) egg-white lysozymes. Agric. Biol. Chem., 54, 2299-2308 (1990).
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 2299-2308
    • Araki, T.1    Kuramoto, M.2    Torikata, T.3
  • 11
    • 0026185391 scopus 로고
    • The amino acid sequence of lysozyme from kalij pheasant (Lophura leucomelana) egg-white
    • Araki, T., Kudo, K., Kuramoto, M., and Torikata, T., The amino acid sequence of lysozyme from kalij pheasant (Lophura leucomelana) egg-white. Agric. Biol. Chem., 55, 1701-1706 (1991).
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 1701-1706
    • Araki, T.1    Kudo, K.2    Kuramoto, M.3    Torikata, T.4
  • 12
    • 0026182768 scopus 로고
    • The amino acid sequence of Reeves' pheasant (Syrmaticus reevesii) lysozyme
    • Araki, T., Kuramoto, M., and Torikata, T., The amino acid sequence of Reeves' pheasant (Syrmaticus reevesii) lysozyme. Agric. Biol. Chem., 55, 1707-1713 (1991).
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 1707-1713
    • Araki, T.1    Kuramoto, M.2    Torikata, T.3
  • 14
    • 0032602266 scopus 로고    scopus 로고
    • The amino acid sequence of wood duck lysozyme
    • Araki, T., and Torikata, T., The amino acid sequence of wood duck lysozyme. Biosci. Biotechnol. Biochem., 63, 220-222 (1999).
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 220-222
    • Araki, T.1    Torikata, T.2
  • 15
    • 0027252943 scopus 로고
    • The primary structures and properties of non-stomach lysozymes of sheep and cow, and implication for functional divergence of lysozyme
    • Ito, Y., Yamada, H., Nakamura, M., Yoshikawa, A., Ueda, T., and Imoto, T., The primary structures and properties of non-stomach lysozymes of sheep and cow, and implication for functional divergence of lysozyme. Eur. J. Biochem., 213, 649-658 (1993).
    • (1993) Eur. J. Biochem. , vol.213 , pp. 649-658
    • Ito, Y.1    Yamada, H.2    Nakamura, M.3    Yoshikawa, A.4    Ueda, T.5    Imoto, T.6
  • 17
    • 0015165106 scopus 로고
    • Human milk lysozyme: Unpublished data concerning the establishment of the complete primary structure; comparison with lysozymes of various origins
    • Jollès, J., and Jollès, P., Human milk lysozyme: unpublished data concerning the establishment of the complete primary structure; comparison with lysozymes of various origins. Helv. Chim. Acta, 54, 2668-2675 (1971).
    • (1971) Helv. Chim. Acta , vol.54 , pp. 2668-2675
    • Jollès, J.1    Jollès, P.2
  • 18
    • 0025877226 scopus 로고
    • cDNA and amino acid sequences of rainbow trout (Oncorhynchus mykiss) lysozymes and their implications for the evolution of lysozyme and lactalbumin
    • Dautigny, A., Prager, E. M., Pham-Dinh, D., Jollès, J., Pakdel, F., Grinde, B., and Jollès. P., cDNA and amino acid sequences of rainbow trout (Oncorhynchus mykiss) lysozymes and their implications for the evolution of lysozyme and lactalbumin. J. Mol. Evol., 32, 187-198 (1991).
    • (1991) J. Mol. Evol. , vol.32 , pp. 187-198
    • Dautigny, A.1    Prager, E.M.2    Pham-Dinh, D.3    Jollès, J.4    Pakdel, F.5    Grinde, B.6    Jollès, P.7
  • 19
    • 0031991117 scopus 로고    scopus 로고
    • Reptile lysozyme: The complete amino acid sequence of soft-shelled turtle lysozyme and its activity
    • Araki, T., Yamamoto, T., and Torikata, T., Reptile lysozyme: The complete amino acid sequence of soft-shelled turtle lysozyme and its activity. Biosci. Biotechnol. Biochem., 62, 316-324 (1998).
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 316-324
    • Araki, T.1    Yamamoto, T.2    Torikata, T.3
  • 20
    • 0029097940 scopus 로고
    • Isolation and characterization of the lysozyme-encoding gene from the silkworm Bombyx mori
    • Lee, W. J., and Brey, P. T., Isolation and characterization of the lysozyme-encoding gene from the silkworm Bombyx mori. Gene, 161, 199-203 (1995).
    • (1995) Gene , vol.161 , pp. 199-203
    • Lee, W.J.1    Brey, P.T.2
  • 21
    • 0026734541 scopus 로고
    • Multiple role for hydrophobicity of tryptophan -108 in chicken lysozyme: Structural stability, saccharide binding ability, and abnormal pKa of glutamic acid -35
    • Inoue, M., Yamada, H., Yasukochi, T., Kuroki, R., Miki, T., Horiuchi, T., and Imoto, T., Multiple role for hydrophobicity of tryptophan -108 in chicken lysozyme: structural stability, saccharide binding ability, and abnormal pKa of glutamic acid -35. Biochemistry, 24, 5545-5553 (1992).
    • (1992) Biochemistry , vol.24 , pp. 5545-5553
    • Inoue, M.1    Yamada, H.2    Yasukochi, T.3    Kuroki, R.4    Miki, T.5    Horiuchi, T.6    Imoto, T.7
  • 22
    • 0032127073 scopus 로고    scopus 로고
    • Structural and functional effect of Trp62Gly and Asp101Gly substitutions on substrate-binding modes of mutant hen egg-white lysozymes
    • Maenaka, K., Matsushima, M., Kawai, G., Kidera, A., Watanabe, K., Kuroki, R., and Kumagai, I., Structural and functional effect of Trp62Gly and Asp101Gly substitutions on substrate-binding modes of mutant hen egg-white lysozymes. Biochem. J., 333, 71-76 (1998).
    • (1998) Biochem. J. , vol.333 , pp. 71-76
    • Maenaka, K.1    Matsushima, M.2    Kawai, G.3    Kidera, A.4    Watanabe, K.5    Kuroki, R.6    Kumagai, I.7
  • 23
    • 0036560170 scopus 로고    scopus 로고
    • Amino acid residues in subsites E and F responsible for the characteristic enzymatic activity of duck egg-white lysozyme
    • Kawamura, S., Toshima, G., Imoto, T., Araki, T., and Torikata, T., Amino acid residues in subsites E and F responsible for the characteristic enzymatic activity of duck egg-white lysozyme. J. Biochem., 131, 663-670 (2002).
    • (2002) J. Biochem. , vol.131 , pp. 663-670
    • Kawamura, S.1    Toshima, G.2    Imoto, T.3    Araki, T.4    Torikata, T.5
  • 24
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • Vocadlo, D. J., Davies, G. J., Laine, R., and Withers, S. G., Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature, 412, 835-838 (2001).
    • (2001) Nature , vol.412 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 27
    • 0027730754 scopus 로고
    • A covalent enzyme substrate intermediate with saccharide distortion in a mutant T4 lysozyme
    • Kuroki, R., Weaver, L. H., and Matthews, B. W., A covalent enzyme substrate intermediate with saccharide distortion in a mutant T4 lysozyme. Science, 262, 2030-2033 (1993).
    • (1993) Science , vol.262 , pp. 2030-2033
    • Kuroki, R.1    Weaver, L.H.2    Matthews, B.W.3
  • 28
    • 0028840318 scopus 로고
    • Structure based design of a lysozyme with alter catalytic activity
    • Kuroki, R., Weaver, L. H., and Matthews, B. W., Structure based design of a lysozyme with alter catalytic activity. Nature Struct. Biol., 11, 1007-1011 (1995).
    • (1995) Nature Struct. Biol. , vol.11 , pp. 1007-1011
    • Kuroki, R.1    Weaver, L.H.2    Matthews, B.W.3
  • 29
    • 0027093322 scopus 로고
    • Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects in both structure and stability
    • Zhang, X. J., Baase, W. A., and Matthews, B. W., Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects in both structure and stability. Protein Sci., 1, 761-776 (1992).
    • (1992) Protein Sci. , vol.1 , pp. 761-776
    • Zhang, X.J.1    Baase, W.A.2    Matthews, B.W.3
  • 30
  • 31
    • 0031893269 scopus 로고    scopus 로고
    • The response of T4 lysozyme to large-to small substitutions with in the core and its relation to the hydrophobic effect
    • Xu, J., Baase, W. A., Baldwin, E., and Matthews, B. W., The response of T4 lysozyme to large-to small substitutions with in the core and its relation to the hydrophobic effect. Protein Sci., 7, 158-177 (1998).
    • (1998) Protein Sci. , vol.7 , pp. 158-177
    • Xu, J.1    Baase, W.A.2    Baldwin, E.3    Matthews, B.W.4
  • 32
    • 0019335167 scopus 로고
    • Complete amino acid sequence of the goose-type lysozyme from the egg white of the black swan
    • Richard, J. S., Geoffrey, S. B., Donna, S. D., and Francis, J. M., Complete amino acid sequence of the goose-type lysozyme from the egg white of the black swan. Biochemistry, 19, 1814-1819 (1980).
    • (1980) Biochemistry , vol.19 , pp. 1814-1819
    • Richard, J.S.1    Geoffrey, S.B.2    Donna, S.D.3    Francis, J.M.4
  • 33
    • 0020122109 scopus 로고
    • Complete amino acid sequence of ostrich (Struthio camelus) egg-white lysozyme, a goose type lysozyme
    • Schoentgen, F., Jollès, J., and Jollès, P., Complete amino acid sequence of ostrich (Struthio camelus) egg-white lysozyme, a goose type lysozyme. Eur. J. Biochem., 123, 489-497 (1982).
    • (1982) Eur. J. Biochem. , vol.123 , pp. 489-497
    • Schoentgen, F.1    Jollès, J.2    Jollès, P.3
  • 35
    • 0025949805 scopus 로고
    • Goose-type lysozyme gene of the chicken: Sequence, genomic organization and expression reveals major differences to chicken-type lysozyme gene
    • Nakano, T., and Graf, T., Goose-type lysozyme gene of the chicken: sequence, genomic organization and expression reveals major differences to chicken-type lysozyme gene. Biochim. Biophys. Acta, 1090, 273-276 (1991).
    • (1991) Biochim. Biophys. Acta , vol.1090 , pp. 273-276
    • Nakano, T.1    Graf, T.2
  • 36
    • 0035973859 scopus 로고    scopus 로고
    • Molecular cloning, expression and evolution of the Japanese flounder goose-type lysozyme gene, and the lytic activity of its recombinant protein
    • Hikima, J., Minagawa, S., Hirono, I., and Aoki, T., Molecular cloning, expression and evolution of the Japanese flounder goose-type lysozyme gene, and the lytic activity of its recombinant protein. Biochim. Biophys. Acta, 30, 35-44 (2001).
    • (2001) Biochim. Biophys. Acta , vol.30 , pp. 35-44
    • Hikima, J.1    Minagawa, S.2    Hirono, I.3    Aoki, T.4
  • 37
    • 4544378457 scopus 로고    scopus 로고
    • Molecular cloning, expression on the goose-type lysozyme cDNA from orange-spotted grouper (Epinephelus coioides), and the lytic activity of its recombinant protein
    • Yin, S., Weng, S., Deng, W., and He, J., Molecular cloning, expression on the goose-type lysozyme cDNA from orange-spotted grouper (Epinephelus coioides), and the lytic activity of its recombinant protein. Aquaculture Asia, 3, 21-22 (2002).
    • (2002) Aquaculture Asia , vol.3 , pp. 21-22
    • Yin, S.1    Weng, S.2    Deng, W.3    He, J.4
  • 38
    • 0016288414 scopus 로고
    • Widespread distribution of lysozyme g in egg white of birds
    • Prager, E. M., Wilson, A. C., and Arnheim, N., Widespread distribution of lysozyme g in egg white of birds. J. Biol. Chem., 249, 7295-7297 (1974).
    • (1974) J. Biol. Chem. , vol.249 , pp. 7295-7297
    • Prager, E.M.1    Wilson, A.C.2    Arnheim, N.3
  • 39
    • 0016218678 scopus 로고
    • Isozymes of lysozyme in leukocytes and egg white: Evidence for the species-specific control of egg-white lysozyme synthesis
    • Hindenburg, A., Spitznagel, J., and Arnheim, N., Isozymes of lysozyme in leukocytes and egg white: evidence for the species-specific control of egg-white lysozyme synthesis. Proc. Natl. Acad. Sci. USA, 71, 1653-1657 (1974).
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 1653-1657
    • Hindenburg, A.1    Spitznagel, J.2    Arnheim, N.3
  • 40
    • 0029687175 scopus 로고    scopus 로고
    • Animal lysozymes c and g: An overview
    • ed. Jollès, P., Birkhäuser verlag basel, Switzerland
    • Prager, E. M., and Jollès, P., Animal lysozymes c and g: an overview. In "Lysozymes: Model Enzymes in Biochemistry and Biology", ed. Jollès, P., Birkhäuser verlag basel, Switzerland, pp. 9-31 (1996).
    • (1996) Lysozymes: Model Enzymes in Biochemistry and Biology , pp. 9-31
    • Prager, E.M.1    Jollès, P.2
  • 41
    • 0028794520 scopus 로고
    • The refined structures of goose lysozyme and its complex with trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue
    • Weaver, L. H., Grütter, M. G., and Matthews, B. W., The refined structures of goose lysozyme and its complex with trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue. J. Mol. Biol., 245, 54-68 (1995).
    • (1995) J. Mol. Biol. , vol.245 , pp. 54-68
    • Weaver, L.H.1    Grütter, M.G.2    Matthews, B.W.3
  • 42
    • 0032517353 scopus 로고    scopus 로고
    • Substrate binding subsites of chitinase from barley seeds and lysozyme from goose egg white
    • Honda, Y., and Fukamizo, T., Substrate binding subsites of chitinase from barley seeds and lysozyme from goose egg white. Biochim. Biophys. Acta, 1388, 53-65 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1388 , pp. 53-65
    • Honda, Y.1    Fukamizo, T.2
  • 43
    • 0019467025 scopus 로고
    • Crystallographic determination of the mode of binding of oligosaccharides to T4 bacteriophage lysozyme: Implications for the mechanism of catalysis
    • Anderson, W. F., Grütter, M. G., Remington, S. J., and Matthews, B. W., Crystallographic determination of the mode of binding of oligosaccharides to T4 bacteriophage lysozyme: implications for the mechanism of catalysis. J. Mol. Biol., 147, 523-543 (1981).
    • (1981) J. Mol. Biol. , vol.147 , pp. 523-543
    • Anderson, W.F.1    Grütter, M.G.2    Remington, S.J.3    Matthews, B.W.4
  • 44
    • 0021713792 scopus 로고
    • Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolution
    • Weaver, L. H., Grütter, M. G., Remington, S. J., Gray, T. M., Isaacs, N. W., and Matthews, B. W., Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolution. J. Mol. Evol., 21, 97-111 (1985).
    • (1985) J. Mol. Evol. , vol.21 , pp. 97-111
    • Weaver, L.H.1    Grütter, M.G.2    Remington, S.J.3    Gray, T.M.4    Isaacs, N.W.5    Matthews, B.W.6
  • 45
    • 0030032332 scopus 로고    scopus 로고
    • Chitinases, chitosanases, and lysozymes can be divided into procaryotic and eucaryotic families sharing a conserved core
    • Monzingo, A. F., Marcotte, E. M., Hart, P. J., and Robertus, J. D., Chitinases, chitosanases, and lysozymes can be divided into procaryotic and eucaryotic families sharing a conserved core. Nature Struct. Biol., 3, 133-140 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 133-140
    • Monzingo, A.F.1    Marcotte, E.M.2    Hart, P.J.3    Robertus, J.D.4
  • 46
    • 0035292701 scopus 로고    scopus 로고
    • Purification and characterization of goose type lysozyme from cassowary (Casuarius casuarius) egg white
    • Thammasirirak, S., Torikata, T., Takami, K., Murata, K., and Araki, T., Purification and characterization of goose type lysozyme from cassowary (Casuarius casuarius) egg white. Biosci. Biotechnol. Biochem., 65, 584-592 (2001).
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 584-592
    • Thammasirirak, S.1    Torikata, T.2    Takami, K.3    Murata, K.4    Araki, T.5
  • 47
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 277, 680-685 (1970).
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 48
    • 0345346100 scopus 로고
    • The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins
    • Crestfield, A. M., Moore, S., and Stein, W. H., The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J. Biol. Chem., 238, 622-627 (1963).
    • (1963) J. Biol. Chem. , vol.238 , pp. 622-627
    • Crestfield, A.M.1    Moore, S.2    Stein, W.H.3
  • 49
    • 0014799475 scopus 로고
    • An internal standard for amino acid analyses: S-beta-(4-pyridylethyl)-L- cysteine
    • Cavins, J. F., and Friedman, M., An internal standard for amino acid analyses: S-beta-(4-pyridylethyl)-L-cysteine. Anal. Biochem., 35, 489-493 (1970).
    • (1970) Anal. Biochem. , vol.35 , pp. 489-493
    • Cavins, J.F.1    Friedman, M.2
  • 50
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins, D., Thompson, J., Gibson, T., Thompson, J. D., Higgins, D. G., and Gibson, T. J., Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6
  • 52
    • 0037287049 scopus 로고    scopus 로고
    • Expression of a synthetic gene coding for ostrich egg-white lysozyme in Pichia pastoris and its enzymatic activity
    • Kawamura, S., Fukamizo, T., Araki, T., and Torikata, T., Expression of a synthetic gene coding for ostrich egg-white lysozyme in Pichia pastoris and its enzymatic activity. J. Biochem., 133, 123-131 (2003).
    • (2003) J. Biochem. , vol.133 , pp. 123-131
    • Kawamura, S.1    Fukamizo, T.2    Araki, T.3    Torikata, T.4
  • 53
    • 0041421103 scopus 로고    scopus 로고
    • Histidine-114 at subsites E and F can explain the characteristic enzymatic activity of guinea hen egg-white lysozyme
    • Toshima, G., Kawamura, S., Araki, T., and Torikata, T., Histidine-114 at subsites E and F can explain the characteristic enzymatic activity of guinea hen egg-white lysozyme. Biosci. Biotechnol. Biochem., 67, 540-546 (2003).
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 540-546
    • Toshima, G.1    Kawamura, S.2    Araki, T.3    Torikata, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.