메뉴 건너뛰기




Volumn 36, Issue 2, 2004, Pages 254-262

Determination of the complete cDNA sequence, construction of expression systems, and elucidation of fibrinolytic activity for Tapes japonica lysozyme

Author keywords

Bi functional; Expression; Fibrinolytic; Folding; Invertebrate type lysozyme

Indexed keywords

CHITINASE; COMPLEMENTARY DNA; ISOPEPTIDASE; LYASE; LYSOZYME;

EID: 3142643627     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.05.001     Document Type: Article
Times cited : (29)

References (32)
  • 5
    • 0016592228 scopus 로고
    • The lysozyme from Asterias rubens
    • Jollès J., Jollès P. The lysozyme from Asterias rubens. Eur. J. Biochem. 54:1975;19-23
    • (1975) Eur. J. Biochem. , vol.54 , pp. 19-23
    • Jollès, J.1    Jollès, P.2
  • 6
    • 0021490172 scopus 로고
    • What's new in lysozyme research? Always a model system, today as yesterday
    • Jollès J., Jollès P. What's new in lysozyme research? Always a model system, today as yesterday. Mol. Cell. Biochem. 63:1984;165-189
    • (1984) Mol. Cell. Biochem. , vol.63 , pp. 165-189
    • Jollès, J.1    Jollès, P.2
  • 10
    • 0029686292 scopus 로고    scopus 로고
    • Molecular evolution of ruminant lysozyme
    • P. Jollès. Basel, Switzerland: Birkhäuser
    • Irwin D.M. Molecular evolution of ruminant lysozyme. Jollès P. Lysozyme: Model Enzymes in Biochemistry and Biology. 1996;347-361 Birkhäuser, Basel, Switzerland
    • (1996) Lysozyme: Model Enzymes in Biochemistry and Biology , pp. 347-361
    • Irwin, D.M.1
  • 12
    • 0033402852 scopus 로고    scopus 로고
    • Protein purification and gene isolation of chlamysin, a cold-active lysozyme-like enzyme with antibacterial activity
    • December 31, 10618496
    • Nilsen I.W., Overbo K., Sandsdalen E., Sandaker E., Sletten K., Myrnes B. Protein purification and gene isolation of chlamysin, a cold-active lysozyme-like enzyme with antibacterial activity. FEBS Lett. 464(3):1999;153-158. December 31, 10618496
    • (1999) FEBS Lett. , vol.464 , Issue.3 , pp. 153-158
    • Nilsen, I.W.1    Overbo, K.2    Sandsdalen, E.3    Sandaker, E.4    Sletten, K.5    Myrnes, B.6
  • 13
    • 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. 259:1999;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
  • 15
    • 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. CMLS. 60:2003;1944-1951
    • (2003) CMLS , vol.60 , pp. 1944-1951
    • Takeshita, K.1    Hashimoto, Y.2    Ueda, T.3    Imoto, T.4
  • 16
    • 0017680149 scopus 로고
    • The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases
    • Folk J.E., Finlayson J.E. The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases. Adv. Prot. Chem. 31:1977;1-133
    • (1977) Adv. Prot. Chem. , vol.31 , pp. 1-133
    • Folk, J.E.1    Finlayson, J.E.2
  • 17
    • 0028322985 scopus 로고
    • Transglutaminases: Protein cross-linking enzymes in tissues and body fluids
    • Aeschlimann D., Paulsson M. Transglutaminases: protein cross-linking enzymes in tissues and body fluids. Thromb. Haemost. 71:1994;402-415
    • (1994) Thromb. Haemost. , vol.71 , pp. 402-415
    • Aeschlimann, D.1    Paulsson, M.2
  • 18
    • 0015788202 scopus 로고
    • The effect of plasmin on the subunit structure of human fibrin
    • Pizzo S.V., Schwartz M.L., Hill R.L., McKee P.A. The effect of plasmin on the subunit structure of human fibrin. J. Biol. Chem. 248:1973;4574-4583
    • (1973) J. Biol. Chem. , vol.248 , pp. 4574-4583
    • Pizzo, S.V.1    Schwartz, M.L.2    Hill, R.L.3    McKee, P.A.4
  • 20
    • 0018726056 scopus 로고
    • A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines
    • Kearney J.F., Randburch A., Liesegang B., Rajewsky K. A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines. J. Immunol. 123:1979;1548-1550
    • (1979) J. Immunol. , vol.123 , pp. 1548-1550
    • Kearney, J.F.1    Randburch, A.2    Liesegang, B.3    Rajewsky, K.4
  • 21
    • 0031415310 scopus 로고    scopus 로고
    • Improvement of the refolding yield and solubility of hen egg-white lysozyme by altering the Met residue attached to its N-terminus to Ser
    • Mine S., Ueda T., Hashimoto Y., Imoto T. Improvement of the refolding yield and solubility of hen egg-white lysozyme by altering the Met residue attached to its N-terminus to Ser. Protein Eng. 10(11):1997;1333-1338
    • (1997) Protein Eng. , vol.10 , Issue.11 , pp. 1333-1338
    • Mine, S.1    Ueda, T.2    Hashimoto, Y.3    Imoto, T.4
  • 22
    • 0028917544 scopus 로고
    • Effective renaturation of reduced lysozyme by gentle removal of urea
    • Maeda Y., Koga H., Yamada H., Ueda T., Imoto T. Effective renaturation of reduced lysozyme by gentle removal of urea. Protein Eng. 8(2):1995;201-205
    • (1995) Protein Eng. , vol.8 , Issue.2 , pp. 201-205
    • Maeda, Y.1    Koga, H.2    Yamada, H.3    Ueda, T.4    Imoto, T.5
  • 23
    • 0024402332 scopus 로고
    • Enhanced bacteriolytic activity of hen egg-white lysozyme due to conversion of Trp62 to other aromatic amino acid residues
    • Kumagai I., Miura K. Enhanced bacteriolytic activity of hen egg-white lysozyme due to conversion of Trp62 to other aromatic amino acid residues. J. Biochem. 105:1989;946-948
    • (1989) J. Biochem. , vol.105 , pp. 946-948
    • Kumagai, I.1    Miura, K.2
  • 24
    • 22644448913 scopus 로고    scopus 로고
    • Destabilase from the medicinal leech: The hydrolysis of isopeptide bonds in D-dimer, a fragment of stabilized fibrin
    • I.P. Baskova, L.L. Zavalova, Basanova, O.V. Grigor'eva, Destabilase from the medicinal leech: the hydrolysis of isopeptide bonds in D-dimer, a fragment of stabilized fibrin, Russ. J. Bioorganic Chem. 25 (1999) 383-386
    • (1999) Russ. J. Bioorganic Chem. , vol.25 , pp. 383-386
    • Baskova, I.P.1    Zavalova, L.L.2    Basanova3    Grigor'eva, O.V.4
  • 25
    • 0344815737 scopus 로고
    • Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid
    • Hirel P.H., Schmitter M.J., Dessen P., Fayat G., Blanquet S. Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid. Proc. Natl. Acad. Sci. USA. 86:1989;8247-8251
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8247-8251
    • Hirel, P.H.1    Schmitter, M.J.2    Dessen, P.3    Fayat, G.4    Blanquet, S.5
  • 26
    • 0027016691 scopus 로고
    • Expression of a group II phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus in Escherichia coli: Recovery and renaturation from bacterial inclusion bodies
    • Lathrop B.K., Burack W.R., Biltonen R.L., Rule G.S. Expression of a group II phospholipase A2 from the venom of Agkistrodon piscivorus piscivorus in Escherichia coli: recovery and renaturation from bacterial inclusion bodies. Protein Expr. Purif. 3:1992;512-517
    • (1992) Protein Expr. Purif. , vol.3 , pp. 512-517
    • Lathrop, B.K.1    Burack, W.R.2    Biltonen, R.L.3    Rule, G.S.4
  • 27
    • 0021713896 scopus 로고
    • Isolation of the putative structural gene for the lysine-arginine- cleaving endopeptidase required for processing of yeast prepro-α-factor
    • David J., Anthony B., Lindley B., Riyo K., Jeremy T. Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factor. Cell. 37:1984;1075-1089
    • (1984) Cell , vol.37 , pp. 1075-1089
    • David, J.1    Anthony, B.2    Lindley, B.3    Riyo, K.4    Jeremy, T.5
  • 28
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast
    • Joan L.C., James M.C. Heterologous protein expression in the methylotrophic yeast. Pichia pastoris FEMS Microbiol. Rev. 24:2000;45-66
    • (2000) Pichia Pastoris FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Joan, L.C.1    James, M.C.2
  • 30
    • 0034060883 scopus 로고    scopus 로고
    • Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris
    • Goda S., Takano K., Yamagata Y., Katakura Y., Yutani K. Effect of extra N-terminal residues on the stability and folding of human lysozyme expressed in Pichia pastoris. Protein Eng. 13(4):2000;299-307
    • (2000) Protein Eng. , vol.13 , Issue.4 , pp. 299-307
    • Goda, S.1    Takano, K.2    Yamagata, Y.3    Katakura, Y.4    Yutani, K.5
  • 31
    • 0029857709 scopus 로고    scopus 로고
    • Genes from the medicinal leech (Hirudo medicinalis) coding for unusual enzymes that specially cleave endo-ε(γ-Glu)-Lys isopeptide bonds and help dissolve blood clots
    • Zavalova L., Lukyanov S., Baskova I., Snezhkov E., Akopov S., Berezhnoy S., Bogdanova E., Basova E., Sverdlov E. Genes from the medicinal leech (Hirudo medicinalis) coding for unusual enzymes that specially cleave endo-ε(γ-Glu)-Lys isopeptide bonds and help dissolve blood clots. Mol. Gen. Genet. 253:1996;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    Basova, E.8    Sverdlov, E.9
  • 32
    • 0033548650 scopus 로고    scopus 로고
    • Analysis of the relationship between enzyme activity and its internal motion using nuclear magnetic resonance: 15N relaxation studies of wild-type and mutant lysozyme
    • Mine S., Tate T.S., Ueda T., Kainosho M., Imoto T. Analysis of the relationship between enzyme activity and its internal motion using nuclear magnetic resonance: 15N relaxation studies of wild-type and mutant lysozyme. J. Mol. Biol. 286:1999;1547-1565
    • (1999) J. Mol. Biol. , vol.286 , pp. 1547-1565
    • Mine, S.1    Tate, T.S.2    Ueda, T.3    Kainosho, M.4    Imoto, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.