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Volumn 41, Issue 11, 2008, Pages 969-977

Cloning, purification and comparative characterization of two digestive lysozymes from Musca domestica larvae

Author keywords

Digestive lysozyme; Lysozyme; pH optimum; Substrate affinity

Indexed keywords

LYSOZYME; PROTEIN MDL1; PROTEIN MDL2; UNCLASSIFIED DRUG;

EID: 59849111960     PISSN: 0100879X     EISSN: 1414431X     Source Type: Journal    
DOI: 10.1590/S0100-879X2008001100005     Document Type: Article
Times cited : (25)

References (32)
  • 2
    • 0025778735 scopus 로고
    • Lysozyme revisited: Crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D
    • Strynadka NC, James MN. Lysozyme revisited: crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D. J Mol Biol 1991; 220: 401-424.
    • (1991) J Mol Biol , vol.220 , pp. 401-424
    • Strynadka, N.C.1    James, M.N.2
  • 3
    • 0013852463 scopus 로고
    • Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution
    • Blake CC, Koenig DF, Mair GA, North AC, Phillips DC, Sarma VR. Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution. Nature 1965; 206: 757-761.
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.4    Phillips, D.C.5    Sarma, V.R.6
  • 4
    • 0000916620 scopus 로고
    • The hen egg-white lysozyme molecule
    • Phillips DC. The hen egg-white lysozyme molecule. Proc Natl Acad Sci U S A 1967; 57: 484-495.
    • (1967) Proc Natl Acad Sci U S A , vol.57 , pp. 484-495
    • Phillips, D.C.1
  • 5
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • Davies GJ, Wilson KS, Henrissat B. Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J 1997; 321 (Part 2): 557-559.
    • (1997) Biochem J , vol.321 , Issue.PART 2 , pp. 557-559
    • Davies, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 6
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • Vocadlo DJ, Davies GJ, Laine R, Withers SG. Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature 2001; 412: 835-838.
    • (2001) Nature , vol.412 , pp. 835-838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 7
    • 0021285423 scopus 로고
    • Stomach lysozymes of ruminants. I. Distribution and catalytic properties
    • Dobson DE, Prager EM, Wilson AC. Stomach lysozymes of ruminants. I. Distribution and catalytic properties. J Biol Chem 1984; 259: 11607-11616.
    • (1984) J Biol Chem , vol.259 , pp. 11607-11616
    • Dobson, D.E.1    Prager, E.M.2    Wilson, A.C.3
  • 8
    • 0023479419 scopus 로고
    • Sequence convergence and functional adaptation of stomach lysozymes from foregut fermenters
    • Stewart CB, Wilson AC. Sequence convergence and functional adaptation of stomach lysozymes from foregut fermenters. Cold Spring Harb Symp Quant Biol 1987; 52: 891-899.
    • (1987) Cold Spring Harb Symp Quant Biol , vol.52 , pp. 891-899
    • Stewart, C.B.1    Wilson, A.C.2
  • 9
    • 0028046864 scopus 로고
    • Molecular adaptation of a leaf-eating bird: Stomach lysozyme of the hoatzin
    • Kornegay JR, Schilling JW, Wilson AC. Molecular adaptation of a leaf-eating bird: stomach lysozyme of the hoatzin. Mol Biol Evol 1994; 11: 921-928.
    • (1994) Mol Biol Evol , vol.11 , pp. 921-928
    • Kornegay, J.R.1    Schilling, J.W.2    Wilson, A.C.3
  • 10
    • 0025940660 scopus 로고
    • Digestion of bacteria and the role of midgut lysozyme in some insect larvae
    • Lemos FJ, Terra WR. Digestion of bacteria and the role of midgut lysozyme in some insect larvae. Comp Biochem Physiol B 1991; 100: 265-268.
    • (1991) Comp Biochem Physiol B , vol.100 , pp. 265-268
    • Lemos, F.J.1    Terra, W.R.2
  • 12
    • 0032078495 scopus 로고    scopus 로고
    • Molecular adaptation of Drosophila melanogaster lysozymes to a digestive function
    • Regel R, Matioli SR, Terra WR. Molecular adaptation of Drosophila melanogaster lysozymes to a digestive function. Insect Biochem Mol Biol 1998; 28: 309-319.
    • (1998) Insect Biochem Mol Biol , vol.28 , pp. 309-319
    • Regel, R.1    Matioli, S.R.2    Terra, W.R.3
  • 13
    • 0000218183 scopus 로고
    • A bacteria-digesting midgut-lysozyme from Musca domestica (Diptera) larvae. Purification, properties and secretory mechanism
    • Lemos FJA, Ribeiro AF, Terra WR. A bacteria-digesting midgut-lysozyme from Musca domestica (Diptera) larvae. Purification, properties and secretory mechanism. Insect Biochem Mol Biol 1993; 23: 533-541.
    • (1993) Insect Biochem Mol Biol , vol.23 , pp. 533-541
    • Lemos, F.J.A.1    Ribeiro, A.F.2    Terra, W.R.3
  • 14
    • 34548617867 scopus 로고    scopus 로고
    • The crystal structure of a lysozyme c from housefly Musca domestica, the first structure of a digestive lysozyme
    • Cançado FC, Valerio AA, Marana SR, Barbosa JA. The crystal structure of a lysozyme c from housefly Musca domestica, the first structure of a digestive lysozyme. J Struct Biol 2007; 160: 83-92.
    • (2007) J Struct Biol , vol.160 , pp. 83-92
    • Cançado, F.C.1    Valerio, A.A.2    Marana, S.R.3    Barbosa, J.A.4
  • 15
    • 0029689666 scopus 로고    scopus 로고
    • Adaptative evolution of lysozyme: Changes in amino acid sequence, regulation of expression and gene number
    • Jollès P Editor, Basel: Birkhauser Verlag;
    • Prager EM. Adaptative evolution of lysozyme: Changes in amino acid sequence, regulation of expression and gene number. In: Jollès P (Editor), Lysozymes: model enzymes in biochemistry and biology. Basel: Birkhauser Verlag; 1996. p 323-345.
    • (1996) Lysozymes: Model enzymes in biochemistry and biology , pp. 323-345
    • Prager, E.M.1
  • 16
    • 0001481948 scopus 로고
    • Rapid amplification of cDNA ends
    • Dieffenbach CW, Dveksler GS Editors, New York: Cold Spring Harbor Laboratory Press;
    • Frohman MA. Rapid amplification of cDNA ends. In: Dieffenbach CW, Dveksler GS (Editors), PCR primer - A laboratory manual. New York: Cold Spring Harbor Laboratory Press; 1995.
    • (1995) PCR primer - A laboratory manual
    • Frohman, M.A.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum H, Beier H, Gross H. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 1987; 8: 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.3
  • 19
    • 0014195281 scopus 로고
    • Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels
    • Shapiro AL, Vinuela E, Maizel JV Jr. Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem Biophys Res Commun 1967; 28: 815-820.
    • (1967) Biochem Biophys Res Commun , vol.28 , pp. 815-820
    • Shapiro, A.L.1    Vinuela, E.2    Maizel Jr., J.V.3
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0003314571 scopus 로고
    • Buffers of pH 2 to 12 for use in electrophoresis
    • Miller GL, Golder RH. Buffers of pH 2 to 12 for use in electrophoresis. Arch Biochem 1950; 29: 420-423.
    • (1950) Arch Biochem , vol.29 , pp. 420-423
    • Miller, G.L.1    Golder, R.H.2
  • 23
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997; 25: 4876-4882.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 24
    • 0029080152 scopus 로고
    • Insect lysozyme from house fly ( Musca domestica) larvae: Possible digestive function based on sequence and enzymatic properties
    • Ito Y, Nakamura M, Hotani T, Imoto T. Insect lysozyme from house fly ( Musca domestica) larvae: possible digestive function based on sequence and enzymatic properties. J Biochem 1995; 118: 546-551.
    • (1995) J Biochem , vol.118 , pp. 546-551
    • Ito, Y.1    Nakamura, M.2    Hotani, T.3    Imoto, T.4
  • 25
    • 0014687514 scopus 로고
    • The dependence of lysozyme activity on pH and ionic strength
    • Davies RC, Neuberger A, Wilson BM. The dependence of lysozyme activity on pH and ionic strength. Biochim Biophys Acta 1969; 178: 294-305.
    • (1969) Biochim Biophys Acta , vol.178 , pp. 294-305
    • Davies, R.C.1    Neuberger, A.2    Wilson, B.M.3
  • 26
    • 0014941891 scopus 로고
    • Influence of pH and ionic strength of the lysis of Micrococcus lysodeikticus cells by six human and four avian lysozymes
    • Saint-Blancard J, Chuzel P, Mathieu Y, Perrot J, Jolles P. Influence of pH and ionic strength of the lysis of Micrococcus lysodeikticus cells by six human and four avian lysozymes. Biochim Biophys Acta 1970; 220: 300-306.
    • (1970) Biochim Biophys Acta , vol.220 , pp. 300-306
    • Saint-Blancard, J.1    Chuzel, P.2    Mathieu, Y.3    Perrot, J.4    Jolles, P.5
  • 27
    • 0017235451 scopus 로고
    • Catalytic implications of electrostatic potentials: The lytic activity of lysozymes as a model
    • Maurel P, Douzou P. Catalytic implications of electrostatic potentials: the lytic activity of lysozymes as a model. J Mol Biol 1976; 102: 253-264.
    • (1976) J Mol Biol , vol.102 , pp. 253-264
    • Maurel, P.1    Douzou, P.2
  • 28
    • 0022996121 scopus 로고
    • Surface charge measurements on Micrococcus lysodeikticus and the catalytic implications for lysozyme
    • Price JA, Pethig R. Surface charge measurements on Micrococcus lysodeikticus and the catalytic implications for lysozyme. Biochim Biophys Acta 1986; 889: 128-135.
    • (1986) Biochim Biophys Acta , vol.889 , pp. 128-135
    • Price, J.A.1    Pethig, R.2
  • 30
    • 0026524571 scopus 로고
    • The lysozyme locus in Drosophila melanogaster: Different genes are expressed in midgut and salivary glands
    • Kylsten P, Kimbrell DA, Daffre S, Samakovlis C, Hultmark D. The lysozyme locus in Drosophila melanogaster: different genes are expressed in midgut and salivary glands. Mol Gen Genet 1992; 232: 335-343.
    • (1992) Mol Gen Genet , vol.232 , pp. 335-343
    • Kylsten, P.1    Kimbrell, D.A.2    Daffre, S.3    Samakovlis, C.4    Hultmark, D.5
  • 31
    • 0028057562 scopus 로고
    • The lysozyme locus in Drosophila melanogaster: An expanded gene family adapted for expression in the digestive tract
    • Daffre S, Kylsten P, Samakovlis C, Hultmark D. The lysozyme locus in Drosophila melanogaster: an expanded gene family adapted for expression in the digestive tract. Mol Gen Genet 1994; 242: 152-162.
    • (1994) Mol Gen Genet , vol.242 , pp. 152-162
    • Daffre, S.1    Kylsten, P.2    Samakovlis, C.3    Hultmark, D.4
  • 32
    • 0032146553 scopus 로고    scopus 로고
    • A lysozyme in the salivary glands of the malaria vector Anopheles darlingi
    • Moreira-Ferro CK, Daffre S, James AA, Marinotti O. A lysozyme in the salivary glands of the malaria vector Anopheles darlingi. Insect Mol Biol 1998; 7: 257-264.
    • (1998) Insect Mol Biol , vol.7 , pp. 257-264
    • Moreira-Ferro, C.K.1    Daffre, S.2    James, A.A.3    Marinotti, O.4


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