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Volumn 64, Issue 21, 2007, Pages 2841-2847

A cold-active salmon goose-type lysozyme with high heat tolerance

Author keywords

Atlantic salmon; Cold active; Gene; Goose type; Immunity; Lysozyme; Protein; Thermal tolerance

Indexed keywords

CYSTEINE; LYSOZYME;

EID: 38549125019     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-007-7372-8     Document Type: Article
Times cited : (53)

References (31)
  • 1
    • 0021490172 scopus 로고
    • What's new in lysozyme research?
    • Jollès, J. and Jollès, P. (1984) What's new in lysozyme research? Mol. Cell. Biochem. 63, 165-189.
    • (1984) Mol. Cell. Biochem , vol.63 , pp. 165-189
    • Jollès, J.1    Jollès, P.2
  • 3
    • 0016592228 scopus 로고
    • The lysozyme from Asterias ruben
    • Jollès, J. and Jollès, P. (1975) The lysozyme from Asterias ruben. Eur. J. Biochem. 54, 19-23.
    • (1975) Eur. J. Biochem , vol.54 , pp. 19-23
    • Jollès, J.1    Jollès, P.2
  • 4
    • 0000646464 scopus 로고
    • On a remarkable bacteriolytic element found in tissues and secretions
    • Flemming, A. (1922) On a remarkable bacteriolytic element found in tissues and secretions. Proc. R. Soc. Lond. B 39, 306-317.
    • (1922) Proc. R. Soc. Lond. B , vol.39 , pp. 306-317
    • Flemming, A.1
  • 5
    • 0014197552 scopus 로고
    • Purification and characterisation of a lysozyme from goose egg white
    • Canfield, R. E. and McMurry, S. (1967) Purification and characterisation of a lysozyme from goose egg white. Biochem. Biophys. Res. Commun. 26, 38-42.
    • (1967) Biochem. Biophys. Res. Commun , vol.26 , pp. 38-42
    • Canfield, R.E.1    McMurry, S.2
  • 6
    • 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-i., Minagawa, S., Hirono, I. and Aoki, T. (2001) Molecular cloning, expression and evolution of the Japanese flounder goose-type lysozyme gene, and the lytic activity of its recombinant protein. Biochim. Biophys. Acta 1520, 35-44.
    • (2001) Biochim. Biophys. Acta , vol.1520 , pp. 35-44
    • Hikima, J.-I.1    Minagawa, S.2    Hirono, I.3    Aoki, T.4
  • 7
    • 0043074437 scopus 로고    scopus 로고
    • Molecular cloning of G type lysozyme cDNA in common carp (Cyprinus carpio L.)
    • Savan, R., Aman, A. and Sakai, M. (2003) Molecular cloning of G type lysozyme cDNA in common carp (Cyprinus carpio L.). Fish Shellfish Immunol. 15, 263-268.
    • (2003) Fish Shellfish Immunol , vol.15 , pp. 263-268
    • Savan, R.1    Aman, A.2    Sakai, M.3
  • 8
    • 0042267811 scopus 로고    scopus 로고
    • Molecular cloning, expression of orange-spotted grouper goose-type lysozyme cDNA, and lytic activity of its recombinant protein
    • Yin, Z. X., He, J. G., Deng, W. X. and Chan, S. M. (2003) Molecular cloning, expression of orange-spotted grouper goose-type lysozyme cDNA, and lytic activity of its recombinant protein. Dis. Aquat. Org. 55, 117-123.
    • (2003) Dis. Aquat. Org , vol.55 , pp. 117-123
    • Yin, Z.X.1    He, J.G.2    Deng, W.X.3    Chan, S.M.4
  • 9
    • 0037309920 scopus 로고    scopus 로고
    • Molecular evolution of vertebrate goose-type lysozyme genes
    • Irwin, D. M. and Gong, Z. (2003) Molecular evolution of vertebrate goose-type lysozyme genes. J. Mol. Evol. 56, 234-242.
    • (2003) J. Mol. Evol , vol.56 , pp. 234-242
    • Irwin, D.M.1    Gong, Z.2
  • 10
    • 0242288826 scopus 로고    scopus 로고
    • Urochordates carry multiple genes for goose-type lysozyme and no genes for chicken- or invertebrate-type lysozymes
    • Nilsen, I. W., Myrnes, B., Edvardsen, R. B. and Chourrout, D. (2003) Urochordates carry multiple genes for goose-type lysozyme and no genes for chicken- or invertebrate-type lysozymes. Cell. Mol. Life Sci. 60, 2210-2218.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 2210-2218
    • Nilsen, I.W.1    Myrnes, B.2    Edvardsen, R.B.3    Chourrout, D.4
  • 11
    • 23444440822 scopus 로고    scopus 로고
    • Zou, H., Song, L., Xu, W. and Yang, G. (2005) Molecular cloning and characterization analysis of cDNA encoding g-type lysozyme from scallop (Argopecten irradians). High Tech. Lett. 15, 101-106.
    • Zou, H., Song, L., Xu, W. and Yang, G. (2005) Molecular cloning and characterization analysis of cDNA encoding g-type lysozyme from scallop (Argopecten irradians). High Tech. Lett. 15, 101-106.
  • 12
    • 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. (1991) Goose-type lysozyme gene of the chicken: Sequence, genomic organization and expression reveals major differences to chicken-type lysozyme gene. Biochem. Biophys. Acta 1090, 273-276.
    • (1991) Biochem. Biophys. Acta , vol.1090 , pp. 273-276
    • Nakano, T.1    Graf, T.2
  • 13
    • 32344443468 scopus 로고    scopus 로고
    • Gene structure of goose-type lysozyme in the mandarin fish Siniperca chuatsi with analysis on the lytic activity of its recombinant in Escherichia coli
    • Sun, B. J., Wang, G. L., Xie, H. X., Gao, Q. and Nie, P. (2006) Gene structure of goose-type lysozyme in the mandarin fish Siniperca chuatsi with analysis on the lytic activity of its recombinant in Escherichia coli. Aquaculture 252, 106-113.
    • (2006) Aquaculture , vol.252 , pp. 106-113
    • Sun, B.J.1    Wang, G.L.2    Xie, H.X.3    Gao, Q.4    Nie, P.5
  • 14
    • 0025885633 scopus 로고
    • Murein-metabolizing enzymes from Escherichia coli: Sequence analysis and overexpression of the slt gene, which encodes the soluble lytic transglycosylase
    • Keck, W., Kazemier, B. and Engel, H. (1991) Murein-metabolizing enzymes from Escherichia coli: sequence analysis and overexpression of the slt gene, which encodes the soluble lytic transglycosylase. J. Bacteriol. 173, 6773-6782.
    • (1991) J. Bacteriol , vol.173 , pp. 6773-6782
    • Keck, W.1    Kazemier, B.2    Engel, H.3
  • 15
    • 0028174847 scopus 로고
    • A conserved domain in putative bacterial and bacteriophage transglycosylases
    • Koonin, E. V. and Rudd, K. E. (1994) A conserved domain in putative bacterial and bacteriophage transglycosylases. Trends Biochem. Sci. 19, 106-107.
    • (1994) Trends Biochem. Sci , vol.19 , pp. 106-107
    • Koonin, E.V.1    Rudd, K.E.2
  • 16
    • 0033402852 scopus 로고    scopus 로고
    • Protein purification and gene isolation of chlamysin, a cold-active lysozyme-like enzyme with antibacterial activity
    • Nilsen, I. W., Øverbø, K., Sandsdalen, E., Sandaker, E., Sletten, K. and Myrnes, B. (1999) Protein purification and gene isolation of chlamysin, a cold-active lysozyme-like enzyme with antibacterial activity. FEBS Lett. 464, 153-158.
    • (1999) FEBS Lett , vol.464 , pp. 153-158
    • Nilsen, I.W.1    Øverbø, K.2    Sandsdalen, E.3    Sandaker, E.4    Sletten, K.5    Myrnes, B.6
  • 17
    • 0025272240 scopus 로고
    • Rapid and sensitive sequence comparison with FASTP and FASTA
    • Pearson, W. R. (1990) Rapid and sensitive sequence comparison with FASTP and FASTA. Meth. Enzymol. 183, 63-98.
    • (1990) Meth. Enzymol , vol.183 , pp. 63-98
    • Pearson, W.R.1
  • 18
    • 0035166973 scopus 로고    scopus 로고
    • Apweiler, R., Attwood, T. K., Bairoch, A., Bateman, A., Birney, E., Biswas, M., Bucher, P., Cerutti, L., Corpet, F., Croning, M. D. R., Durbin, R., Falquet, L., Fleischmann, W., Gouzy, J., Hermjakob, H., Hulo, N., Jonassen, I., Kahn, D., Kanapin, A., Karavidopoulou, Y., Lopez, R., Marx, B., Mulder, N. J., Oinn, T. M., Pagni, M., Servant, F., Sigrist, C. J. A. and Zdobnov, E. M. (2001) The InterPro database, an integrated documentation resource for protein families, domains and functional sites. Nucleic Acids Res. 29, 37-40.
    • Apweiler, R., Attwood, T. K., Bairoch, A., Bateman, A., Birney, E., Biswas, M., Bucher, P., Cerutti, L., Corpet, F., Croning, M. D. R., Durbin, R., Falquet, L., Fleischmann, W., Gouzy, J., Hermjakob, H., Hulo, N., Jonassen, I., Kahn, D., Kanapin, A., Karavidopoulou, Y., Lopez, R., Marx, B., Mulder, N. J., Oinn, T. M., Pagni, M., Servant, F., Sigrist, C. J. A. and Zdobnov, E. M. (2001) The InterPro database, an integrated documentation resource for protein families, domains and functional sites. Nucleic Acids Res. 29, 37-40.
  • 19
  • 20
    • 0025744474 scopus 로고
    • Prediction of human mRNA donor and acceptor sites from the DNA sequence
    • Brunak, S., Engelbrecht, J., and Knudsen, S. (1991) Prediction of human mRNA donor and acceptor sites from the DNA sequence. J. Mol. Biol. 220, 49-65.
    • (1991) J. Mol. Biol , vol.220 , pp. 49-65
    • Brunak, S.1    Engelbrecht, J.2    Knudsen, S.3
  • 21
    • 0035292701 scopus 로고    scopus 로고
    • Purification and characterization of goose type lysozyme from Cassovary (Casuarius casuarius) egg white
    • Thammasirirak, S., Torikata, T., Takami, K., Murata, K. and Araki, T. (2001) Purification and characterization of goose type lysozyme from Cassovary (Casuarius casuarius) egg white. Biosci. Biotechnol. Biochem. 65, 584-592.
    • (2001) Biosci. Biotechnol. Biochem , vol.65 , pp. 584-592
    • Thammasirirak, S.1    Torikata, T.2    Takami, K.3    Murata, K.4    Araki, T.5
  • 24
    • 0037688133 scopus 로고    scopus 로고
    • Molecular adaptations to cold in psycrophilic enzymes
    • Feller, G. (2003) Molecular adaptations to cold in psycrophilic enzymes. Cell. Mol. Life Sci. 60, 648-662.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 648-662
    • Feller, G.1
  • 26
    • 34249920434 scopus 로고
    • Characterization of a pancreatic DNase from pyloric caeca of Atlantic cod (Gadus morhua)
    • Strætkvern, K. O., Raae, A. J. and Walther,, B. T. (1992) Characterization of a pancreatic DNase from pyloric caeca of Atlantic cod (Gadus morhua). Fish Physiol. Biochem. 9, 439-452.
    • (1992) Fish Physiol. Biochem , vol.9 , pp. 439-452
    • Strætkvern, K.O.1    Raae, A.J.2    Walther, B.T.3
  • 27
    • 0028873872 scopus 로고
    • Alkaline phosphatase from Atlantic cod (Gadus morhua). Kinetic and structural properties which indicate adaptation to low temperatures
    • Ásgeirsson, B., Hartemink, R. and Chlebowski, J. F. (1995) Alkaline phosphatase from Atlantic cod (Gadus morhua). Kinetic and structural properties which indicate adaptation to low temperatures. Comp. Biochem. Physiol. Biochem. 110, 315-329.
    • (1995) Comp. Biochem. Physiol. Biochem , vol.110 , pp. 315-329
    • Ásgeirsson, B.1    Hartemink, R.2    Chlebowski, J.F.3
  • 28
    • 0036484727 scopus 로고    scopus 로고
    • Identification, cloning, and expression of uracil-DNA glycosylase from Atlantic cod (Gadus morhua): Characterization and homology modeling of the cold-active catalytic domain
    • Lanes, O., Leiros, I., Smal-s, A.O. and Willassen, N. P. (2002) Identification, cloning, and expression of uracil-DNA glycosylase from Atlantic cod (Gadus morhua): characterization and homology modeling of the cold-active catalytic domain. Extremophiles 6, 73-86.
    • (2002) Extremophiles , vol.6 , pp. 73-86
    • Lanes, O.1    Leiros, I.2    Smal-s, A.O.3    Willassen, N.P.4
  • 29
    • 0029851195 scopus 로고    scopus 로고
    • Temperature and pH sensitivity of trypsins from Atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsin
    • Outzen, H., Berglund, G. I., Smal-s, A. O. and Willassen, N. P. (1996) Temperature and pH sensitivity of trypsins from Atlantic salmon (Salmo salar) in comparison with bovine and porcine trypsin. Comp. Biochem. Physiol. Biochem. 115, 33-45.
    • (1996) Comp. Biochem. Physiol. Biochem , vol.115 , pp. 33-45
    • Outzen, H.1    Berglund, G.I.2    Smal-s, A.O.3    Willassen, N.P.4
  • 30
    • 0032102873 scopus 로고    scopus 로고
    • Purification and characterization of pancreatic elastase from North Atlantic salmon (Salmo salar)
    • Berglund, G. I., Smal-s, A. O., Outzen, H. and Willassen, N. P. (1998) Purification and characterization of pancreatic elastase from North Atlantic salmon (Salmo salar). Mol. Mar. Biol. Biotechnol. 7: 105-114.
    • (1998) Mol. Mar. Biol. Biotechnol , vol.7 , pp. 105-114
    • Berglund, G.I.1    Smal-s, A.O.2    Outzen, H.3    Willassen, N.P.4
  • 31
    • 11144252652 scopus 로고    scopus 로고
    • Identification and characterization of a highly thermostable bacteriophage lysozyme
    • Lavigne, R., Briers, Y., Hertveldt, K., Robben, J. and Volckaert, G. (2004) Identification and characterization of a highly thermostable bacteriophage lysozyme. Cell. Mol. Life Sci. 61, 2753-2759.
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 2753-2759
    • Lavigne, R.1    Briers, Y.2    Hertveldt, K.3    Robben, J.4    Volckaert, G.5


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