메뉴 건너뛰기




Volumn 28, Issue 5-6, 1998, Pages 309-319

Molecular adaptation of Drosophila melanogaster lysozymes to a digestive function

Author keywords

Digestive lysozyme; Lysozyme properties; Lysozyme purification; Lysozyme sequences; Ruminant lysozyme

Indexed keywords

LYSOZYME;

EID: 0032078495     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(97)00108-2     Document Type: Article
Times cited : (86)

References (47)
  • 1
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum H., Beir H., Gross H. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis. 8:1987;93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beir, H.2    Gross, H.3
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analyt. Biochem. 72:1976;248-254.
    • (1976) Analyt. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0023814379 scopus 로고
    • Cloning the human lysozyme cDNA: Inverted Alu repeat in the mRNA and in situ hybridization for macrophages and Paneth cells
    • Chung L. P., Keshav S., Gordon S. Cloning the human lysozyme cDNA: inverted Alu repeat in the mRNA and in situ hybridization for macrophages and Paneth cells. Proc. Natl. Acad. Sci. USA. 85:1988;6227-6231.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6227-6231
    • Chung, L.P.1    Keshav, S.2    Gordon, S.3
  • 4
    • 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. 242:1994;152-162.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 152-162
    • Daffre, S.1    Kylsten, P.2    Samakovlis, C.3    Hultmark, D.4
  • 5
    • 0021285423 scopus 로고
    • Stomach lysozymes of ruminants. I. Distribution and catalytic properties
    • Dobson D. E., Prager E. M., Wilson A. C. Stomach lysozymes of ruminants. I. Distribution and catalytic properties. J. Biol. Chem. 259:1984;11607-11616.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11607-11616
    • Dobson, D.E.1    Prager, E.M.2    Wilson, A.C.3
  • 6
    • 0001341405 scopus 로고
    • Biochemical aspects of insect immunology
    • Dunn P. E. Biochemical aspects of insect immunology. A. Rev. Ent. 31:1986;321-339.
    • (1986) A. Rev. Ent. , vol.31 , pp. 321-339
    • Dunn, P.E.1
  • 7
    • 0000127901 scopus 로고
    • Amino acid and cDNA sequences of lysozyme from Hyalophora cecropia
    • Engström A., Xanthopoulos K. G., Boman H. G., Bennich H. Amino acid and cDNA sequences of lysozyme from Hyalophora cecropia. EMBO J. 4:1985;2119-2122.
    • (1985) EMBO J. , vol.4 , pp. 2119-2122
    • Engström, A.1    Xanthopoulos, K.G.2    Boman, H.G.3    Bennich, H.4
  • 9
    • 70449274093 scopus 로고
    • Persistence of bacteria in the developmental stages of the housefly. II. Quantitative study of the host-contaminant relationship in flies breeding under natural conditions
    • Greenberg B. Persistence of bacteria in the developmental stages of the housefly. II. Quantitative study of the host-contaminant relationship in flies breeding under natural conditions. Am. J. Trop. Med. Hyg. 8:1959;412-416.
    • (1959) Am. J. Trop. Med. Hyg. , vol.8 , pp. 412-416
    • Greenberg, B.1
  • 10
    • 0000207265 scopus 로고
    • Confidence limits on the maximum likelihood estimation of the hominoid tree from mitochondrial DNA sequences
    • Hasegawa M., Kishino H. Confidence limits on the maximum likelihood estimation of the hominoid tree from mitochondrial DNA sequences. Evolution. 43:1989;672-677.
    • (1989) Evolution , vol.43 , pp. 672-677
    • Hasegawa, M.1    Kishino, H.2
  • 12
    • 77956935682 scopus 로고
    • Vertebrate Lysozymes
    • In: Boyer, P. D. (Ed.), Academic Press, New York
    • Imoto, T., Johnson, L. N., North, A. C. T., Phillips, D. C. and Rupley, J. A. 1972. Vertebrate Lysozymes. In: Boyer, P. D. (Ed.), The Enzymes, Vol. 7, Academic Press, New York, pp. 665-868.
    • (1972) The Enzymes , vol.7 , pp. 665-868
    • Imoto, T.1    Johnson, L.N.2    North, A.C.T.3    Phillips, D.C.4    Rupley, J.A.5
  • 13
    • 0024361632 scopus 로고
    • Multiple cDNA sequences and the evolution of bovine stomach lysozyme
    • Irwin D. M., Wilson A. C. Multiple cDNA sequences and the evolution of bovine stomach lysozyme. J. Biol. Chem. 264:1989;11387-11393.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11387-11393
    • Irwin, D.M.1    Wilson, A.C.2
  • 14
    • 0025261112 scopus 로고
    • Concerted evolution of ruminant stomach lysozymes: Characterization of lysozyme cDNA clones from sheep and deer
    • Irwin D. M., Wilson A. C. Concerted evolution of ruminant stomach lysozymes: characterization of lysozyme cDNA clones from sheep and deer. J. Biol. Chem. 265:1990;4944-4952.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4944-4952
    • Irwin, D.M.1    Wilson, A.C.2
  • 15
    • 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. Tokyo. 118:1995;546-551.
    • (1995) J. Biochem. Tokyo , vol.118 , pp. 546-551
    • Ito, Y.1    Nakamura, M.2    Hotani, T.3    Imoto, T.4
  • 17
    • 0021126597 scopus 로고
    • Stomach lysozymes of ruminants. II. Amino acid sequence of cow lysozyme 2 and immunological comparisons with other lysozymes
    • Jollès P., Schoentgen F., Jollès J., Dobson D. E., Prager E. M., Wilson A. C. Stomach lysozymes of ruminants. II. Amino acid sequence of cow lysozyme 2 and immunological comparisons with other lysozymes. J. Biol. Chem. 259:1984;11617-11625.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11617-11625
    • Jollès, P.1    Schoentgen, F.2    Jollès, J.3    Dobson, D.E.4    Prager, E.M.5    Wilson, A.C.6
  • 20
    • 0026524571 scopus 로고
    • The lysozyme locus in Drosophila melanogaster: Different genes are expressed in midgut and salivary glands
    • Kylsten P., Kimbrell D. A., Daffre S., Samakovlis C., Hultmark D. The lysozyme locus in Drosophila melanogaster: different genes are expressed in midgut and salivary glands. Molec. Gen. Genet. 232:1992;335-343.
    • (1992) Molec. Gen. Genet. , vol.232 , pp. 335-343
    • Kylsten, P.1    Kimbrell, D.A.2    Daffre, S.3    Samakovlis, C.4    Hultmark, D.5
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0029097940 scopus 로고
    • Isolation and characterization of the lysozyme-encoding gene from the silkworm Bombyx mori
    • Lee W. J., Brey P. T. Isolation and characterization of the lysozyme-encoding gene from the silkworm Bombyx mori. Gene. 161:1995;199-203.
    • (1995) Gene , vol.161 , pp. 199-203
    • Lee, W.J.1    Brey, P.T.2
  • 23
    • 0025940660 scopus 로고
    • Digestion of bacteria and the role of midgut lysozyme in some insect larvae
    • Lemos F. J. A., Terra W. R. Digestion of bacteria and the role of midgut lysozyme in some insect larvae. Comp. Biochem. Physiol. 100B:1991;265-268.
    • (1991) Comp. Biochem. Physiol. , vol.100 , pp. 265-268
    • Lemos, F.J.A.1    Terra, W.R.2
  • 24
    • 0000358169 scopus 로고
    • Properties and intracellular distribution of a cathepsin D-like proteinase active at the acid region of Musca domestica midgut
    • Lemos F. J. A., Terra W. R. Properties and intracellular distribution of a cathepsin D-like proteinase active at the acid region of Musca domestica midgut. Insect Biochem. 21:1991;457-465.
    • (1991) Insect Biochem. , vol.21 , pp. 457-465
    • Lemos, F.J.A.1    Terra, W.R.2
  • 25
    • 0000218183 scopus 로고
    • A bacteria-digesting midgut-lysozyme from Musca domestica (Diptera) larvae. Purification, properties and secretory mechanism
    • Lemos F. J. A., Ribeiro A. F., Terra W. R. A bacteria-digesting midgut-lysozyme from Musca domestica (Diptera) larvae. Purification, properties and secretory mechanism. Insect Biochem. Molec. Biol. 23:1993;533-541.
    • (1993) Insect Biochem. Molec. Biol. , vol.23 , pp. 533-541
    • Lemos, F.J.A.1    Ribeiro, A.F.2    Terra, W.R.3
  • 26
    • 73049130725 scopus 로고
    • A method for determining the sedimentation behavior of enzymes: Application to protein mixtures
    • Martin R. G., Ames B. N. A method for determining the sedimentation behavior of enzymes: application to protein mixtures. J. Biol. Chem. 236:1961;1372-1379.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1372-1379
    • Martin, R.G.1    Ames, B.N.2
  • 27
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidine difluoride membranes
    • Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidine difluoride membranes. J. Biol. Chem. 262:1987;10035-10038.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 28
    • 0030047527 scopus 로고    scopus 로고
    • Is Aspartate 52 essential for catalysis by chicken egg white lysozyme? The role of natural substrate-assisted hydrolysis
    • Matsumura I., Kirsch J. F. Is Aspartate 52 essential for catalysis by chicken egg white lysozyme? The role of natural substrate-assisted hydrolysis. Biochemistry. 35:1996;1881-1889.
    • (1996) Biochemistry , vol.35 , pp. 1881-1889
    • Matsumura, I.1    Kirsch, J.F.2
  • 29
    • 0017235451 scopus 로고
    • Catalytic implications of electrostatic potentials: The lytic activity of lysozyme as a model
    • Maurel P., Douzou P. Catalytic implications of electrostatic potentials: the lytic activity of lysozyme as a model. J. Molec. Biol. 102:1976;253-264.
    • (1976) J. Molec. Biol. , vol.102 , pp. 253-264
    • Maurel, P.1    Douzou, P.2
  • 31
    • 0003314571 scopus 로고
    • Buffers of pH 2 to 12 for use in electrophoresis
    • Miller G. L., Golder R. H. Buffers of pH 2 to 12 for use in electrophoresis. Arch. Biochem. 29:1950;420-423.
    • (1950) Arch. Biochem. , vol.29 , pp. 420-423
    • Miller, G.L.1    Golder, R.H.2
  • 32
    • 0026622867 scopus 로고
    • Modifications of the bicinchoninic acid protein assay to eliminate lipid interference in determining lipoprotein protein content
    • Morton R. E., Evans T. A. Modifications of the bicinchoninic acid protein assay to eliminate lipid interference in determining lipoprotein protein content. Anal. Biochem. 204:1992;332-334.
    • (1992) Anal. Biochem. , vol.204 , pp. 332-334
    • Morton, R.E.1    Evans, T.A.2
  • 33
    • 0028385708 scopus 로고
    • Structure and induction of a lysozyme gene from the tobacco hornworm Manduca sexta
    • Mulnix A. M., Dunn P. E. Structure and induction of a lysozyme gene from the tobacco hornworm Manduca sexta. Insect Biochem. Molec. Biol. 24:1994;271-281.
    • (1994) Insect Biochem. Molec. Biol. , vol.24 , pp. 271-281
    • Mulnix, A.M.1    Dunn, P.E.2
  • 34
    • 0020108288 scopus 로고
    • Calf rennet lysozyme
    • Pahud J.J., Widmer F. Calf rennet lysozyme. Biochem. J. 201:1982;661-664.
    • (1982) Biochem. J. , vol.201 , pp. 661-664
    • Pahud, J.J.1    Widmer, F.2
  • 35
    • 0029689666 scopus 로고    scopus 로고
    • Adaptive evolution of lysozyme: Changes in amino acid sequence, regulation of expression and gene number
    • In Jollès, P. (Ed.), Birkhäuser Verlag, Basel
    • Prager, E. M. 1996. Adaptive evolution of lysozyme: changes in amino acid sequence, regulation of expression and gene number. In Jollès, P. (Ed.), Lysozymes: Model Enzymes in Biochemistry and Biology, Birkhäuser Verlag, Basel, pp. 323-345.
    • (1996) Lysozymes: Model Enzymes in Biochemistry and Biology , pp. 323-345
    • Prager, E.M.1
  • 36
    • 0014195281 scopus 로고
    • Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels
    • Shapiro A. L., Viñuela E., Maizel J. V. Jr. Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem. Biophys. Res. Commun. 28:1967;815-820.
    • (1967) Biochem. Biophys. Res. Commun. , vol.28 , pp. 815-820
    • Shapiro, A.L.1    Viñuela, E.2    Maizel J.V., Jr.3
  • 38
    • 0023479419 scopus 로고
    • Sequence convergence and functional adaptation of stomach lysozymes from foregut fermenters
    • Stewart C. B., Wilson A. C. Sequence convergence and functional adaptation of stomach lysozymes from foregut fermenters. Cold Spring Harb. Symp. Quant. Biol. 52:1987;891-899.
    • (1987) Cold Spring Harb. Symp. Quant. Biol. , vol.52 , pp. 891-899
    • Stewart, C.B.1    Wilson, A.C.2
  • 39
    • 0023666025 scopus 로고
    • Adaptive evolution in the stomach lysozymes of foregut fermenters
    • Stewart C. B., Schilling J. W., Wilson A. C. Adaptive evolution in the stomach lysozymes of foregut fermenters. Nature. 330:1987;401-404.
    • (1987) Nature , vol.330 , pp. 401-404
    • Stewart, C.B.1    Schilling, J.W.2    Wilson, A.C.3
  • 40
    • 0025809272 scopus 로고
    • Organization and expression of the immunoresponsive lysozyme gene in the giant silk moth Hyalophora cecropia
    • Sun S. C., Asling B., Faye I. Organization and expression of the immunoresponsive lysozyme gene in the giant silk moth Hyalophora cecropia. J. Biol. Chem. 266:1991;6644-6649.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6644-6649
    • Sun, S.C.1    Asling, B.2    Faye, I.3
  • 42
    • 0025671095 scopus 로고
    • Evolution of digestive systems of insects
    • Terra W. R. Evolution of digestive systems of insects. A. Rev. Ent. 35:1990;181-200.
    • (1990) A. Rev. Ent. , vol.35 , pp. 181-200
    • Terra, W.R.1
  • 43
    • 0017893171 scopus 로고
    • Physical properties and Tris inhibition of an insect trehalase and a thermodynamic approach to the nature of its active site
    • Terra W. R., Ferreira C., De Bianchi A. G. Physical properties and Tris inhibition of an insect trehalase and a thermodynamic approach to the nature of its active site. Biochim. Biophys. Acta. 524:1978;131-141.
    • (1978) Biochim. Biophys. Acta , vol.524 , pp. 131-141
    • Terra, W.R.1    Ferreira, C.2    De Bianchi, A.G.3
  • 44
    • 0000198740 scopus 로고
    • Further evidence that enzymes involved in the final stages of digestion of Rhynchosciara americana do not enter the endoperitrophic space
    • Terra W. R., Ferreira C. Further evidence that enzymes involved in the final stages of digestion of Rhynchosciara americana do not enter the endoperitrophic space. Insect Biochem. 13:1983;143-150.
    • (1983) Insect Biochem. , vol.13 , pp. 143-150
    • Terra, W.R.1    Ferreira, C.2
  • 45
    • 0027999854 scopus 로고
    • Insect digestive enzymes: Properties, compartmentalization and function
    • Terra W. R., Ferreira C. Insect digestive enzymes: properties, compartmentalization and function. Comp. Biochem. Physiol. 109B:1994;1-62.
    • (1994) Comp. Biochem. Physiol. , vol.109 , pp. 1-62
    • Terra, W.R.1    Ferreira, C.2
  • 46
    • 0016108920 scopus 로고
    • Chitinase activity during Drosophila development
    • Winicur S., Mitchell H. K. Chitinase activity during Drosophila development. J. Insect Physiol. 20:1974;1775-1805.
    • (1974) J. Insect Physiol. , vol.20 , pp. 1775-1805
    • Winicur, S.1    Mitchell, H.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.