메뉴 건너뛰기




Volumn 41, Issue 2, 2013, Pages 282-294

A bifunctional invertebrate-type lysozyme from the disk abalone, Haliotis discus discus: Genome organization, transcriptional profiling and biological activities of recombinant protein

Author keywords

Genomic structure; Haliotis discus discus; Immune response; Invertebrate type lysozyme; Isopeptidase activity; Lytic activity

Indexed keywords

ABLYSI PROTEIN; ASPARTIC ACID; COMPLEMENTARY DNA; CYSTEINE; GLUTAMIC ACID; ISOPEPTIDASE; LYSOZYME; MESSENGER RNA; PEPTIDASE; RECOMBINANT ENZYME; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 84880630291     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2013.06.009     Document Type: Article
Times cited : (30)

References (64)
  • 1
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 3
    • 51449114870 scopus 로고    scopus 로고
    • Polyfunctionality of destabilase, a lysozyme from a medicinal leech
    • Baskova I.P., Zavalova L.L. Polyfunctionality of destabilase, a lysozyme from a medicinal leech. Bioorg. Khim. 2008, 34:337-343.
    • (2008) Bioorg. Khim. , vol.34 , pp. 337-343
    • Baskova, I.P.1    Zavalova, L.L.2
  • 4
    • 0002788404 scopus 로고
    • Degradation of bacteria by Mytilus edulis
    • Birkbeck T.H., McHenery J.G. Degradation of bacteria by Mytilus edulis. Mar. Biol. 1982, 72:7-15.
    • (1982) Mar. Biol. , vol.72 , pp. 7-15
    • Birkbeck, T.H.1    McHenery, J.G.2
  • 5
    • 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. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 36849047751 scopus 로고    scopus 로고
    • Characterization and identification of virulent Klebsiella oxytoca isolated from abalone (Haliotis diversicolor supertexta) postlarvae with mass mortality in Fujian, China
    • Cai J., Wang Z., Cai C., Zhou Y. Characterization and identification of virulent Klebsiella oxytoca isolated from abalone (Haliotis diversicolor supertexta) postlarvae with mass mortality in Fujian, China. J. Invertebr. Pathol. 2008, 97:70-75.
    • (2008) J. Invertebr. Pathol. , vol.97 , pp. 70-75
    • Cai, J.1    Wang, Z.2    Cai, C.3    Zhou, Y.4
  • 7
    • 77951759131 scopus 로고    scopus 로고
    • Lysozymes in the animal kingdom
    • Callewaert L., Michiels C.W. Lysozymes in the animal kingdom. J. Biosci. 2010, 35:127-160.
    • (2010) J. Biosci. , vol.35 , pp. 127-160
    • Callewaert, L.1    Michiels, C.W.2
  • 8
    • 0002808286 scopus 로고    scopus 로고
    • Enzymes involved in defense functions of hemocytes of mussel mytilus galloprovincialis
    • Carballal M.J., Lopez C., Azevedo C., Villalba A. Enzymes involved in defense functions of hemocytes of mussel mytilus galloprovincialis. J. Invertebr. Pathol. 1997, 70:96-105.
    • (1997) J. Invertebr. Pathol. , vol.70 , pp. 96-105
    • Carballal, M.J.1    Lopez, C.2    Azevedo, C.3    Villalba, A.4
  • 9
    • 22044439259 scopus 로고    scopus 로고
    • Herpes-like virus infection causing mortality of cultured abalone Haliotis diversicolor supertexta in Taiwan
    • Chang P.H., Kuo S.T., Lai S.H., Yang H.S., Ting Y.Y., Hsu C.L., Chen H.C. Herpes-like virus infection causing mortality of cultured abalone Haliotis diversicolor supertexta in Taiwan. Dis. Aquat. Organ. 2005, 65:23-27.
    • (2005) Dis. Aquat. Organ. , vol.65 , pp. 23-27
    • Chang, P.H.1    Kuo, S.T.2    Lai, S.H.3    Yang, H.S.4    Ting, Y.Y.5    Hsu, C.L.6    Chen, H.C.7
  • 10
    • 65549095492 scopus 로고    scopus 로고
    • Characterization of an i-type lysozyme gene from the sea cucumber Stichopus japonicus, and enzymatic and nonenzymatic antimicrobial activities of its recombinant protein
    • Cong L., Yang X., Wang X., Tada M., Lu M., Liu H., Zhu B. Characterization of an i-type lysozyme gene from the sea cucumber Stichopus japonicus, and enzymatic and nonenzymatic antimicrobial activities of its recombinant protein. J. Biosci. Bioeng. 2009, 107:583-588.
    • (2009) J. Biosci. Bioeng. , vol.107 , pp. 583-588
    • Cong, L.1    Yang, X.2    Wang, X.3    Tada, M.4    Lu, M.5    Liu, H.6    Zhu, B.7
  • 12
    • 78650705163 scopus 로고    scopus 로고
    • Molecular characterization of a mollusk chicken-type lysozyme gene from Haliotis discus hannai Ino, and the antimicrobial activity of its recombinant protein
    • Ding J., Li J., Bao Y., Li L., Wu F., Zhang G. Molecular characterization of a mollusk chicken-type lysozyme gene from Haliotis discus hannai Ino, and the antimicrobial activity of its recombinant protein. Fish Shellfish Immunol. 2011, 30:163-172.
    • (2011) Fish Shellfish Immunol. , vol.30 , pp. 163-172
    • Ding, J.1    Li, J.2    Bao, Y.3    Li, L.4    Wu, F.5    Zhang, G.6
  • 13
    • 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. 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
  • 14
    • 50149095793 scopus 로고    scopus 로고
    • The genome sequencer FLX system - longer reads, more applications, straight forward bioinformatics and more complete data sets
    • Droege M., Hill B. The genome sequencer FLX system - longer reads, more applications, straight forward bioinformatics and more complete data sets. J. Biotechnol. 2008, 136:3-10.
    • (2008) J. Biotechnol. , vol.136 , pp. 3-10
    • Droege, M.1    Hill, B.2
  • 15
    • 85004044137 scopus 로고    scopus 로고
    • Pathogenesis of vibriosis in cultured juvenile red abalone, Haliotis rufescens Swainson
    • Elston R., Wood G.S.L. Pathogenesis of vibriosis in cultured juvenile red abalone, Haliotis rufescens Swainson. J. Fish Dis. 2006, 6:111-128.
    • (2006) J. Fish Dis. , vol.6 , pp. 111-128
    • Elston, R.1    Wood, G.S.L.2
  • 16
    • 23144437891 scopus 로고    scopus 로고
    • DiANNA: a web server for disulfide connectivity prediction
    • Ferre F., Clote P. DiANNA: a web server for disulfide connectivity prediction. Nucleic Acids Res. 2005, 33:W230-W232.
    • (2005) Nucleic Acids Res. , vol.33
    • Ferre, F.1    Clote, P.2
  • 17
    • 0001159146 scopus 로고
    • Perkinsus, a protistan parasite of abalone in Australia: a review
    • Goggin C.L., Lester R.J.G. Perkinsus, a protistan parasite of abalone in Australia: a review. Mar. Freshw. Res. 1995, 46:639-646.
    • (1995) Mar. Freshw. Res. , vol.46 , pp. 639-646
    • Goggin, C.L.1    Lester, R.J.G.2
  • 18
    • 84862795082 scopus 로고    scopus 로고
    • A goose-type lysozyme gene in Japanese scallop (Mizuhopecten yessoensis): cDNA cloning, mRNA expression and promoter sequence analysis
    • He C., Yu H., Liu W., Su H., Shan Z., Bao X., Li Y., Fu L., Gao X. A goose-type lysozyme gene in Japanese scallop (Mizuhopecten yessoensis): cDNA cloning, mRNA expression and promoter sequence analysis. Comp. Biochem. Physiol. B: Biochem. Mol. Biol. 2012, 162:34-43.
    • (2012) Comp. Biochem. Physiol. B: Biochem. Mol. Biol. , vol.162 , pp. 34-43
    • He, C.1    Yu, H.2    Liu, W.3    Su, H.4    Shan, Z.5    Bao, X.6    Li, Y.7    Fu, L.8    Gao, X.9
  • 19
    • 0034190077 scopus 로고    scopus 로고
    • Molecular cloning and novel repeated sequences of a C-type lysozyme gene in Japanese Flounder (Paralichthys olivaceus)
    • Hikima J., Hirono I.I., Aoki T. Molecular cloning and novel repeated sequences of a C-type lysozyme gene in Japanese Flounder (Paralichthys olivaceus). Mar. Biotechnol (NY) 2000, 2:241-247.
    • (2000) Mar. Biotechnol (NY) , vol.2 , pp. 241-247
    • Hikima, J.1    Hirono, I.I.2    Aoki, T.3
  • 20
    • 0037309920 scopus 로고    scopus 로고
    • Molecular evolution of vertebrate goose-type lysozyme genes
    • Irwin D.M., Gong Z. Molecular evolution of vertebrate goose-type lysozyme genes. J. Mol. Evol. 2003, 56:234-242.
    • (2003) J. Mol. Evol. , vol.56 , pp. 234-242
    • Irwin, D.M.1    Gong, Z.2
  • 21
    • 0026486022 scopus 로고
    • Evolutionary genetics of ruminant lysozymes
    • Irwin D.M., Prager E.M., Wilson A.C. Evolutionary genetics of ruminant lysozymes. Anim. Genet. 1992, 23:193-202.
    • (1992) Anim. Genet. , vol.23 , pp. 193-202
    • Irwin, D.M.1    Prager, E.M.2    Wilson, A.C.3
  • 22
    • 0035829309 scopus 로고    scopus 로고
    • An outbreak of VHSV (viral hemorrhagic septicemia virus) infection in farmed Japanese flounder Paralichthys olivaceus in Japan
    • Isshik T., Nishizawa T., Kobayashi T., Nagano T., Miyazaki T. An outbreak of VHSV (viral hemorrhagic septicemia virus) infection in farmed Japanese flounder Paralichthys olivaceus in Japan. Dis. Aquat. Organ. 2001, 47:87-99.
    • (2001) Dis. Aquat. Organ. , vol.47 , pp. 87-99
    • Isshik, T.1    Nishizawa, T.2    Kobayashi, T.3    Nagano, T.4    Miyazaki, T.5
  • 23
    • 0033556162 scopus 로고    scopus 로고
    • Amino acid sequences of lysozymes newly purified from invertebrates imply wide distribution of a novel class in the lysozyme family
    • Ito Y., Yoshikawa A., Hotani T., Fukuda S., Sugimura K., Imoto T. Amino acid sequences of lysozymes newly purified from invertebrates imply wide distribution of a novel class in the lysozyme family. Eur. J. Biochem. 1999, 259:456-461.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 456-461
    • Ito, Y.1    Yoshikawa, A.2    Hotani, T.3    Fukuda, S.4    Sugimura, K.5    Imoto, T.6
  • 24
    • 77955058512 scopus 로고    scopus 로고
    • Presence and characterization of multiple mantle lysozymes in the Pacific oyster, Crassostrea gigas
    • Itoh N., Okada Y., Takahashi K.G., Osada M. Presence and characterization of multiple mantle lysozymes in the Pacific oyster, Crassostrea gigas. Fish Shellfish Immunol. 2010, 29:126-135.
    • (2010) Fish Shellfish Immunol. , vol.29 , pp. 126-135
    • Itoh, N.1    Okada, Y.2    Takahashi, K.G.3    Osada, M.4
  • 25
  • 26
    • 0021490172 scopus 로고
    • What's new in lysozyme research? Always a model system, today as yesterday
    • Jolles P., Jolles J. What's new in lysozyme research? Always a model system, today as yesterday. Mol. Cell. Biochem. 1984, 63:165-189.
    • (1984) Mol. Cell. Biochem. , vol.63 , pp. 165-189
    • Jolles, P.1    Jolles, J.2
  • 27
    • 67349280294 scopus 로고    scopus 로고
    • Identification and cloning of an invertebrate-type lysozyme from Eisenia andrei
    • Joskova R., Silerova M., Prochazkova P., Bilej M. Identification and cloning of an invertebrate-type lysozyme from Eisenia andrei. Dev. Comp. Immunol. 2009, 33:932-938.
    • (2009) Dev. Comp. Immunol. , vol.33 , pp. 932-938
    • Joskova, R.1    Silerova, M.2    Prochazkova, P.3    Bilej, M.4
  • 30
    • 53149130940 scopus 로고    scopus 로고
    • The LPS-induced transcriptional upregulation of the chicken lysozyme locus involves CTCF eviction and noncoding RNA transcription
    • Lefevre P., Witham J., Lacroix C.E., Cockerill P.N., Bonifer C. The LPS-induced transcriptional upregulation of the chicken lysozyme locus involves CTCF eviction and noncoding RNA transcription. Mol. Cell 2008, 32:129-139.
    • (2008) Mol. Cell , vol.32 , pp. 129-139
    • Lefevre, P.1    Witham, J.2    Lacroix, C.E.3    Cockerill, P.N.4    Bonifer, C.5
  • 31
    • 0025125790 scopus 로고
    • Differential effects of LPS, IFN-gamma and TNF alpha on the secretion of lysozyme by individual human mononuclear phagocytes: relationship to cell maturity
    • Lewis C.E., McCarthy S.P., Lorenzen J., McGee J.O. Differential effects of LPS, IFN-gamma and TNF alpha on the secretion of lysozyme by individual human mononuclear phagocytes: relationship to cell maturity. Immunology 1990, 69:402-408.
    • (1990) Immunology , vol.69 , pp. 402-408
    • Lewis, C.E.1    McCarthy, S.P.2    Lorenzen, J.3    McGee, J.O.4
  • 32
    • 79551644039 scopus 로고    scopus 로고
    • Immunological studies on Haliotis discus hannai with Vibrio fluvialia II
    • Li T.-W., Ding M., Xiang J.R.L. Immunological studies on Haliotis discus hannai with Vibrio fluvialia II. Oceanol. Limnol. Sin. 1997, 28:27-32.
    • (1997) Oceanol. Limnol. Sin. , vol.28 , pp. 27-32
    • Li, T.-W.1    Ding, M.2    Xiang, J.R.L.3
  • 33
    • 0035222495 scopus 로고    scopus 로고
    • Pathogenicity of Vibrio alginolyticus isolated from diseased small abalone Haliotis diversicolor supertexta
    • Liu P.C., Chen Y.C., Lee K.K. Pathogenicity of Vibrio alginolyticus isolated from diseased small abalone Haliotis diversicolor supertexta. Microbios 2001, 104:71-77.
    • (2001) Microbios , vol.104 , pp. 71-77
    • Liu, P.C.1    Chen, Y.C.2    Lee, K.K.3
  • 34
    • 33344459927 scopus 로고    scopus 로고
    • Characterization, organization and expression of AmphiLysC, an acidic c-type lysozyme gene in amphioxus Branchiostoma belcheri tsingtauense
    • Liu M., Zhang S., Liu Z., Li H., Xu A. Characterization, organization and expression of AmphiLysC, an acidic c-type lysozyme gene in amphioxus Branchiostoma belcheri tsingtauense. Gene 2006, 367:110-117.
    • (2006) Gene , vol.367 , pp. 110-117
    • Liu, M.1    Zhang, S.2    Liu, Z.3    Li, H.4    Xu, A.5
  • 35
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 36
    • 77949916732 scopus 로고    scopus 로고
    • Protection of blue shrimp (Litopenaeus stylirostris) against the White Spot Syndrome Virus (WSSV) when injected with shrimp lysozyme
    • Mai W.J., Wang W.N. Protection of blue shrimp (Litopenaeus stylirostris) against the White Spot Syndrome Virus (WSSV) when injected with shrimp lysozyme. Fish Shellfish Immunol. 2010, 28:727-733.
    • (2010) Fish Shellfish Immunol. , vol.28 , pp. 727-733
    • Mai, W.J.1    Wang, W.N.2
  • 37
    • 0024215242 scopus 로고
    • An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein
    • Maina C.V., Riggs P.D., Grandea A.G., Slatko B.E., Moran L.S., Tagliamonte J.A., McReynolds L.A., Guan C.D. An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein. Gene 1988, 74:365-373.
    • (1988) Gene , vol.74 , pp. 365-373
    • Maina, C.V.1    Riggs, P.D.2    Grandea, A.G.3    Slatko, B.E.4    Moran, L.S.5    Tagliamonte, J.A.6    McReynolds, L.A.7    Guan, C.D.8
  • 39
    • 33845232951 scopus 로고    scopus 로고
    • Cloning of cDNAs and hybridization analysis of lysozymes from two oyster species, Crassostrea gigas and Ostrea edulis
    • Matsumoto T., Nakamura A.M., Takahashi K.G. Cloning of cDNAs and hybridization analysis of lysozymes from two oyster species, Crassostrea gigas and Ostrea edulis. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2006, 145:325-330.
    • (2006) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.145 , pp. 325-330
    • Matsumoto, T.1    Nakamura, A.M.2    Takahashi, K.G.3
  • 40
    • 77957279133 scopus 로고    scopus 로고
    • Activation of c-Myb transcription factor is critical for PMA-induced lysozyme expression in airway epithelial cells
    • Moon U.Y., Bae J.H., Kim C.H., Kim H.J., Kang J.W., Yoon J.H. Activation of c-Myb transcription factor is critical for PMA-induced lysozyme expression in airway epithelial cells. J. Cell. Biochem. 2010, 111:476-487.
    • (2010) J. Cell. Biochem. , vol.111 , pp. 476-487
    • Moon, U.Y.1    Bae, J.H.2    Kim, C.H.3    Kim, H.J.4    Kang, J.W.5    Yoon, J.H.6
  • 41
    • 0028371171 scopus 로고
    • Recovery of lysozyme from scallop waste
    • Myrnes B., Johansen A. Recovery of lysozyme from scallop waste. Prep. Biochem. 1994, 24:69-80.
    • (1994) Prep. Biochem. , vol.24 , pp. 69-80
    • Myrnes, B.1    Johansen, A.2
  • 42
    • 43549090429 scopus 로고    scopus 로고
    • Cloning and molecular characterization of two invertebrate-type lysozymes from Anopheles gambiae
    • Paskewitz S.M., Li B., Kajla M.K. Cloning and molecular characterization of two invertebrate-type lysozymes from Anopheles gambiae. Insect Mol. Biol. 2008, 17:217-225.
    • (2008) Insect Mol. Biol. , vol.17 , pp. 217-225
    • Paskewitz, S.M.1    Li, B.2    Kajla, M.K.3
  • 43
    • 0015514832 scopus 로고
    • The lysozyme from Nephthys hombergi (annelid)
    • Perin J.P., Jolles P. The lysozyme from Nephthys hombergi (annelid). Biochim. Biophys. Acta 1972, 263:683-689.
    • (1972) Biochim. Biophys. Acta , vol.263 , pp. 683-689
    • Perin, J.P.1    Jolles, P.2
  • 44
    • 0025165372 scopus 로고
    • Hydrolytic enzymes associated with the granular haemocytes of the marine mussel Mytilus edulis
    • Pipe R.K. Hydrolytic enzymes associated with the granular haemocytes of the marine mussel Mytilus edulis. Histochem. J. 1990, 22:595-603.
    • (1990) Histochem. J. , vol.22 , pp. 595-603
    • Pipe, R.K.1
  • 46
    • 85027920279 scopus 로고    scopus 로고
    • Genomic characterization and expression profiles upon bacterial infection of a novel cystatin B homologue from disk abalone (Haliotis discus discus)
    • Premachandra H.K., Wan Q., Elvitigala D.A., Zoysa M.D., Choi C.Y., Whang I., Lee J. Genomic characterization and expression profiles upon bacterial infection of a novel cystatin B homologue from disk abalone (Haliotis discus discus). Dev. Comp. Immunol. 2012, 38:495-504.
    • (2012) Dev. Comp. Immunol. , vol.38 , pp. 495-504
    • Premachandra, H.K.1    Wan, Q.2    Elvitigala, D.A.3    Zoysa, M.D.4    Choi, C.Y.5    Whang, I.6    Lee, J.7
  • 47
    • 0030800608 scopus 로고    scopus 로고
    • Molecular divergence of lysozymes and alpha-lactalbumin
    • Qasba P.K., Kumar S. Molecular divergence of lysozymes and alpha-lactalbumin. Crit. Rev. Biochem. Mol. Biol. 1997, 32:255-306.
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 255-306
    • Qasba, P.K.1    Kumar, S.2
  • 48
    • 84862800656 scopus 로고    scopus 로고
    • Identification and expression analysis of goose-type lysozyme in half-smooth tongue sole (Cynoglossus semilaevis)
    • Sha Z.X., Wang Q.L., Liu Y., Chen S.L. Identification and expression analysis of goose-type lysozyme in half-smooth tongue sole (Cynoglossus semilaevis). Fish Shellfish Immunol. 2012, 32:914-921.
    • (2012) Fish Shellfish Immunol. , vol.32 , pp. 914-921
    • Sha, Z.X.1    Wang, Q.L.2    Liu, Y.3    Chen, S.L.4
  • 49
    • 0041386167 scopus 로고    scopus 로고
    • Prediction of potential C/EBP/NF-kappaB composite elements using matrix-based search methods
    • Shelest E., Kel A.E., Goessling E., Wingender E. Prediction of potential C/EBP/NF-kappaB composite elements using matrix-based search methods. In Silico Biol. 2003, 3:71-79.
    • (2003) In Silico Biol. , vol.3 , pp. 71-79
    • Shelest, E.1    Kel, A.E.2    Goessling, E.3    Wingender, E.4
  • 51
    • 76749107386 scopus 로고    scopus 로고
    • Molecular characterization and expression analysis of a c-type and two novel muramidase-deficient i-type lysozymes from Penaeus monodon
    • Supungul P., Rimphanitchayakit V., Aoki T., Hirono I., Tassanakajon A. Molecular characterization and expression analysis of a c-type and two novel muramidase-deficient i-type lysozymes from Penaeus monodon. Fish Shellfish Immunol. 2010, 28:490-498.
    • (2010) Fish Shellfish Immunol. , vol.28 , pp. 490-498
    • Supungul, P.1    Rimphanitchayakit, V.2    Aoki, T.3    Hirono, I.4    Tassanakajon, A.5
  • 52
    • 0141637403 scopus 로고    scopus 로고
    • A small chimerically bifunctional monomeric protein: Tapes japonica lysozyme
    • Takeshita K., Hashimoto Y., Ueda T., Imoto T. A small chimerically bifunctional monomeric protein: Tapes japonica lysozyme. Cell. Mol. Life Sci. 2003, 60:1944-1951.
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1944-1951
    • Takeshita, K.1    Hashimoto, Y.2    Ueda, T.3    Imoto, T.4
  • 53
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K., Peterson D., Peterson N., Stecher G., Nei M., Kumar S. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol. 2011, 28:2731-2739.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 54
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., 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. 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 55
    • 0029052863 scopus 로고
    • The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes
    • Thunnissen A.M., Isaacs N.W., Dijkstra B.W. The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes. Proteins 1995, 22:245-258.
    • (1995) Proteins , vol.22 , pp. 245-258
    • Thunnissen, A.M.1    Isaacs, N.W.2    Dijkstra, B.W.3
  • 57
    • 79551634460 scopus 로고    scopus 로고
    • Characterization and expression analysis of a goose-type lysozyme from the rock bream Oplegnathus fasciatus, and antimicrobial activity of its recombinant protein
    • Whang I., Lee Y., Lee S., Oh M.J., Jung S.J., Choi C.Y., Lee W.S., Kim H.S., Kim S.J., Lee J. Characterization and expression analysis of a goose-type lysozyme from the rock bream Oplegnathus fasciatus, and antimicrobial activity of its recombinant protein. Fish Shellfish Immunol. 2011, 30:532-542.
    • (2011) Fish Shellfish Immunol. , vol.30 , pp. 532-542
    • Whang, I.1    Lee, Y.2    Lee, S.3    Oh, M.J.4    Jung, S.J.5    Choi, C.Y.6    Lee, W.S.7    Kim, H.S.8    Kim, S.J.9    Lee, J.10
  • 59
    • 33846512298 scopus 로고    scopus 로고
    • A new lysozyme from the eastern oyster (Crassostrea virginica) indicates adaptive evolution of i-type lysozymes
    • Xue Q.G., Itoh N., Schey K.L., Li Y.L., Cooper R.K., La Peyre J.F. A new lysozyme from the eastern oyster (Crassostrea virginica) indicates adaptive evolution of i-type lysozymes. Cell. Mol. Life Sci. 2007, 64:82-95.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 82-95
    • Xue, Q.G.1    Itoh, N.2    Schey, K.L.3    Li, Y.L.4    Cooper, R.K.5    La Peyre, J.F.6
  • 60
    • 79551626247 scopus 로고    scopus 로고
    • An i-type lysozyme from the Asiatic hard clam Meretrix meretrix potentially functioning in host immunity
    • Yue X., Liu B., Xue Q. An i-type lysozyme from the Asiatic hard clam Meretrix meretrix potentially functioning in host immunity. Fish Shellfish Immunol. 2011, 30:550-558.
    • (2011) Fish Shellfish Immunol. , vol.30 , pp. 550-558
    • Yue, X.1    Liu, B.2    Xue, Q.3
  • 61
    • 0029857709 scopus 로고    scopus 로고
    • Genes from the medicinal leech (Hirudo medicinalis) coding for unusual enzymes that specifically cleave endo-epsilon (gamma-Glu)-Lys isopeptide bonds and help to dissolve blood clots
    • Zavalova L., Lukyanov S., Baskova I., Snezhkov E., Akopov S., Berezhnoy S., Bogdanova E., Barsova E., Sverdlov E.D. Genes from the medicinal leech (Hirudo medicinalis) coding for unusual enzymes that specifically cleave endo-epsilon (gamma-Glu)-Lys isopeptide bonds and help to dissolve blood clots. Mol. Gen. Genet. 1996, 253:20-25.
    • (1996) Mol. Gen. Genet. , vol.253 , pp. 20-25
    • Zavalova, L.1    Lukyanov, S.2    Baskova, I.3    Snezhkov, E.4    Akopov, S.5    Berezhnoy, S.6    Bogdanova, E.7    Barsova, E.8    Sverdlov, E.D.9
  • 62
    • 33646760651 scopus 로고    scopus 로고
    • Antibacterial non-glycosidase activity of invertebrate destabilase-lysozyme and of its helical amphipathic peptides
    • Zavalova L.L., Yudina T.G., Artamonova I.I., Baskova I.P. Antibacterial non-glycosidase activity of invertebrate destabilase-lysozyme and of its helical amphipathic peptides. Chemotherapy 2006, 52:158-160.
    • (2006) Chemotherapy , vol.52 , pp. 158-160
    • Zavalova, L.L.1    Yudina, T.G.2    Artamonova, I.I.3    Baskova, I.P.4
  • 63
    • 77957750507 scopus 로고    scopus 로고
    • Functional analysis of two invertebrate-type lysozymes from red swamp crayfish, Procambarus clarkii
    • Zhang H.W., Sun C., Sun S.S., Zhao X.F., Wang J.X. Functional analysis of two invertebrate-type lysozymes from red swamp crayfish, Procambarus clarkii. Fish Shellfish Immunol. 2010, 29:1066-1072.
    • (2010) Fish Shellfish Immunol. , vol.29 , pp. 1066-1072
    • Zhang, H.W.1    Sun, C.2    Sun, S.S.3    Zhao, X.F.4    Wang, J.X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.