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Volumn 6, Issue 2, 2012, Pages 203-209

Antifungal and antibacterial functions of medicinal leech recombinant destabilase-lysozyme and its heated-up derivative

Author keywords

antifungal activity; antimicrobial activity; heated up derivative of rec.Dest Lys (T rec.Dest Lys); medicinal leech; recombinant destabilase lysozyme (rec.Dest Lys)

Indexed keywords


EID: 84861761493     PISSN: 20950179     EISSN: 20950187     Source Type: Journal    
DOI: 10.1007/s11705-012-1277-2     Document Type: Article
Times cited : (8)

References (19)
  • 2
    • 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. Bioorganicheskaia Khimiia, 2008, 34(3): 337-343.
    • (2008) Bioorganicheskaia Khimiia , vol.34 , Issue.3 , pp. 337-343
    • Baskova, I.P.1    Zavalova, L.L.2
  • 3
    • 70649097280 scopus 로고    scopus 로고
    • Characterization of the cell wall of the ubiquitous plant pathogen Botrytis cinerea
    • Cantu D, Carl Greve L, Labavitch J M, Powell A L T. Characterization of the cell wall of the ubiquitous plant pathogen Botrytis cinerea. Mycological Research, 2009, 113(12): 1396-1403.
    • (2009) Mycological Research , vol.113 , Issue.12 , pp. 1396-1403
    • Cantu, D.1    Carl Greve, L.2    Labavitch, J.M.3    Powell, A.L.T.4
  • 4
    • 0022992575 scopus 로고
    • Ultrastructure of outermost layer of cell wall in Candida albicans observed by rapid-freezing technique
    • Tokunaga M, Kusamichi M, Koike H. Ultrastructure of outermost layer of cell wall in Candida albicans observed by rapid-freezing technique. Journal of Electron Microscopy, 1986, 35(3): 237-246.
    • (1986) Journal of Electron Microscopy , vol.35 , Issue.3 , pp. 237-246
    • Tokunaga, M.1    Kusamichi, M.2    Koike, H.3
  • 5
    • 7444256327 scopus 로고    scopus 로고
    • The role of proteins in formation of molecular structure of yeast cell wall
    • Kalebina T S, Kulaev I S. The role of proteins in formation of molecular structure of yeast cell wall. Successes of biological chemistry (Moscow), 2001, 41: 105-130.
    • (2001) Successes of Biological Chemistry (Moscow) , vol.41 , pp. 105-130
    • Kalebina, T.S.1    Kulaev, I.S.2
  • 7
    • 0035941271 scopus 로고    scopus 로고
    • A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action
    • Ibrahim H R, Thomas U, Pellegrini A. A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action. The Journal of biological chemistry, 2001, 276(47): 43767-43774.
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.47 , pp. 43767-43774
    • Ibrahim, H.R.1    Thomas, U.2    Pellegrini, A.3
  • 8
    • 36348990220 scopus 로고    scopus 로고
    • Lytic antimicrobial activity of hen egg white lysozyme immobilized to polystyrene beads
    • Wu Y, Daeschel M A. Lytic antimicrobial activity of hen egg white lysozyme immobilized to polystyrene beads. Journal of Food Science, 2007, 72(9): M369-M374.
    • (2007) Journal of Food Science , vol.72 , Issue.9
    • Wu, Y.1    Daeschel, M.A.2
  • 9
    • 0027357549 scopus 로고
    • The in vitro lysozyme susceptibility of Candida species cultured in sucrose supplemented media
    • Samaranayake Y H, MacFarlane TW, Samaranayake L P, Aitchison T C. The in vitro lysozyme susceptibility of Candida species cultured in sucrose supplemented media. Microbios, 1993, 74(298): 23-28.
    • (1993) Microbios , vol.74 , Issue.298 , pp. 23-28
    • Samaranayake, Y.H.1    Macfarlane, T.W.2    Samaranayake, L.P.3    Aitchison, T.C.4
  • 11
    • 33646760651 scopus 로고    scopus 로고
    • Antibacterial non-glycosidase activity of invertebrate destabilaselysozyme and of its helical amphipathic peptides
    • Zavalova L L, Yudina T G, Artamonova I I, Baskova I P. Antibacterial non-glycosidase activity of invertebrate destabilaselysozyme and of its helical amphipathic peptides. Chemotherapy, 2006, 52(3): 158-160.
    • (2006) Chemotherapy , vol.52 , Issue.3 , pp. 158-160
    • Zavalova, L.L.1    Yudina, T.G.2    Artamonova, I.I.3    Baskova, I.P.4
  • 13
    • 84861791194 scopus 로고    scopus 로고
    • The electron microscopy and scanning probe (tunneling) microscopy in microbiology
    • In: Netrusov A I, ed. Moscow
    • Yudina T G, Bogdanov A G. The electron microscopy and scanning probe (tunneling) microscopy in microbiology. In: Netrusov A I, ed. Practical exercises in Microbiology. Moscow, 2005, 83-93.
    • (2005) Practical exercises in Microbiology , pp. 83-93
    • Yudina, T.G.1    Bogdanov, A.G.2
  • 14
    • 33749511435 scopus 로고    scopus 로고
    • Programmed cell death in the aspergilli and other filamentous fungi
    • Robson G D. Programmed cell death in the aspergilli and other filamentous fungi. Medical Mycology, 2006, 44(s1): 109-114.
    • (2006) Medical Mycology , vol.44 , Issue.s1 , pp. 109-114
    • Robson, G.D.1
  • 15
    • 27144540982 scopus 로고    scopus 로고
    • Processing of lysozyme at distinct loops by pepsin: a novel action for generating multiple antimicrobial peptide motifs in the newborn stomach
    • Ibrahim H R, Inazaki D, Abdou A, Aoki T, Kim M. Processing of lysozyme at distinct loops by pepsin: a novel action for generating multiple antimicrobial peptide motifs in the newborn stomach. Biochimica et Biophysica Acta, 2005, 1726(1): 102-114.
    • (2005) Biochimica Et Biophysica Acta , vol.1726 , Issue.1 , pp. 102-114
    • Ibrahim, H.R.1    Inazaki, D.2    Abdou, A.3    Aoki, T.4    Kim, M.5
  • 16
    • 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. Journal of Bioscience and Bioengineering, 2009, 107(6): 583-588.
    • (2009) Journal of Bioscience and Bioengineering , vol.107 , Issue.6 , pp. 583-588
    • Cong, L.1    Yang, X.2    Wang, X.3    Tada, M.4    Lu, M.5    Liu, H.6    Zhu, B.7
  • 17
    • 33745303470 scopus 로고    scopus 로고
    • The peptidoglycandegrading property of lysozyme is not required for bactericidal activity in vivo
    • (Baltimore, MD.:1950)
    • Nash J A, Ballard T N, Weaver T E, Akinbi H T. The peptidoglycandegrading property of lysozyme is not required for bactericidal activity in vivo. Journal of Immunology (Baltimore, MD.: 1950), 2006, 177(1): 519-526.
    • (2006) Journal of Immunology , vol.177 , Issue.1 , pp. 519-526
    • Nash, J.A.1    Ballard, T.N.2    Weaver, T.E.3    Akinbi, H.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.