메뉴 건너뛰기




Volumn 18, Issue 2, 2010, Pages 69-76

Purification and characterization of a novel fibrinolytic protease from Schizophyllum commune

Author keywords

Antithrombotic; Cross flow filtration; Fibrinolytic protease; Mushroom; Schizophyllum commune

Indexed keywords

EDETIC ACID; FIBRINOLYTIC AGENT; FIBRINOLYTIC PROTEASE; MAGNESIUM; PLASMIN; UNCLASSIFIED DRUG;

EID: 77954798853     PISSN: 10219498     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (18)

References (35)
  • 1
    • 0029094814 scopus 로고
    • Thrombosis and the pharmacology of antithrombotic agents
    • Haines, S. T. and Bussey, H. I. 1995. Thrombosis and the pharmacology of antithrombotic agents. Ann. Pharmacother. 29: 892-905.
    • (1995) Ann. Pharmacother. , vol.29 , pp. 892-905
    • Haines, S.T.1    Bussey, H.I.2
  • 2
    • 0037340432 scopus 로고    scopus 로고
    • Molecular mechanisms of initiation of fibrinolysis by fibrin
    • Medved, L. and Nieuwenhuizen, W. 2003. Molecular mechanisms of initiation of fibrinolysis by fibrin. Thromb. Haemost. 89: 409-419.
    • (2003) Thromb. Haemost. , vol.89 , pp. 409-419
    • Medved, L.1    Nieuwenhuizen, W.2
  • 4
    • 33645287745 scopus 로고    scopus 로고
    • Development of new fibrinolytic agents
    • Ueshima, S. and Matsuo, O. 2006. Development of new fibrinolytic agents. Curr. Pharm. Des. 12: 849-857.
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 849-857
    • Ueshima, S.1    Matsuo, O.2
  • 5
    • 0032722442 scopus 로고    scopus 로고
    • The plasminogen (fibrinolytic) system
    • Collen, D. 1999. The plasminogen (fibrinolytic) system. Thromb. Haemost. 82: 259-270.
    • (1999) Thromb. Haemost. , vol.82 , pp. 259-270
    • Collen, D.1
  • 7
    • 34247139742 scopus 로고    scopus 로고
    • Ammodytase, a metalloprotease from Vipera ammodytes ammodytes venom, possesses strong fibrinolytic activity
    • DOI 10.1016/j.toxicon.2006.12.003, PII S0041010106004661
    • Leonardi, A., Fox, J. W., Trampus-Bakija, A. and Krizaj, I. 2007. Ammodytase, a metalloprotease from Vipera ammodytes ammodytes venom, possesses strong fibrinolytic activity. Toxicon. 49: 833-842. (Pubitemid 46590251)
    • (2007) Toxicon , vol.49 , Issue.6 , pp. 833-842
    • Leonardi, A.1    Fox, J.W.2    Trampus-Bakija, A.3    Krizaj, I.4
  • 8
    • 20444379332 scopus 로고    scopus 로고
    • Cloning of thrombolytic enzyme (lumbrokinase) from earthworm and its expression in the yeast Pichia pastoris
    • Ge, T., Sun, Z. J., Fu, S. H. and Liang, G. D. 2005. Cloning of thrombolytic enzyme (lumbrokinase) from earthworm and its expression in the yeast Pichia pastoris. Protein Expr. Purif. 42: 20-28.
    • (2005) Protein Expr. Purif. , vol.42 , pp. 20-28
    • Ge, T.1    Sun, Z.J.2    Fu, S.H.3    Liang, G.D.4
  • 9
    • 29144505132 scopus 로고    scopus 로고
    • Microbial fibrinolytic enzymes: An overview of source, production, properties, and thrombolytic activity in vivo
    • Peng, Y., Yang, X. J. and Zhang, Y. Z. 2005. Microbial fibrinolytic enzymes: an overview of source, production, properties, and thrombolytic activity in vivo. Appl. Microbiol. Biotechnol. 69: 126-132.
    • (2005) Appl. Microbiol. Biotechnol. , vol.69 , pp. 126-132
    • Peng, Y.1    Yang, X.J.2    Zhang, Y.Z.3
  • 10
    • 12344282128 scopus 로고    scopus 로고
    • Fibrinolytic enzymes in Asian traditional fermented foods
    • Mine, Y., Wong, A. H. K. and Jiang, B. 2005. Fibrinolytic enzymes in Asian traditional fermented foods. Food Res. Int. 38: 243-250.
    • (2005) Food Res. Int. , vol.38 , pp. 243-250
    • Mine, Y.1    Wong, A.H.K.2    Jiang, B.3
  • 11
    • 30544431647 scopus 로고    scopus 로고
    • Medicinal mushrooms and cancer therapy: Translating a traditional practice into Western medicine
    • Sullivan, R., Smith, J. E. and Rowan, N. J. 2006. Medicinal mushrooms and cancer therapy: translating a traditional practice into Western medicine. Perspect. Biol. Med. 49: 159-170.
    • (2006) Perspect. Biol. Med. , vol.49 , pp. 159-170
    • Sullivan, R.1    Smith, J.E.2    Rowan, N.J.3
  • 12
    • 2942620243 scopus 로고    scopus 로고
    • Peptides and proteins from fungi
    • Ng, T. B. 2004. Peptides and proteins from fungi. Peptides 25: 1055-1073.
    • (2004) Peptides , vol.25 , pp. 1055-1073
    • Ng, T.B.1
  • 13
    • 0034892635 scopus 로고    scopus 로고
    • Characteristics of a cheese-like food produced by fermentation of the mushroom Schizophyllum commune
    • Okamura-Matsui, T., Takemura, K., Sera, M., Takeno, T., Noda, H., Fukuda, S. and Ohsugi, M. 2001. Characteristics of a cheese-like food produced by fermentation of the mushroom Schizophyllum commune. J. Biosci. Bioeng. 92: 30-32.
    • (2001) J. Biosci. Bioeng. , vol.92 , pp. 30-32
    • Okamura-Matsui, T.1    Takemura, K.2    Sera, M.3    Takeno, T.4    Noda, H.5    Fukuda, S.6    Ohsugi, M.7
  • 14
    • 0347459336 scopus 로고
    • Quantitative enzymic assay of human plasminogen and plasmin with azocasein as substrate
    • Hummel, B. C. W., Schor, J. M., Buck, F. F., Boggiano, E. and De Renzo, E. C. 1965. Quantitative enzymic assay of human plasminogen and plasmin with azocasein as substrate. Anal. Biochem. 11: 532-547.
    • (1965) Anal. Biochem. , vol.11 , pp. 532-547
    • Hummel, B.C.W.1    Schor, J.M.2    Buck, F.F.3    Boggiano, E.4    De Renzo, E.C.5
  • 15
    • 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. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 50449151040 scopus 로고
    • The fibrin plate method for estimating fibrinolytic activity
    • Astrup, T. and Mullertz, S. 1952. The fibrin plate method for estimating fibrinolytic activity. Arch. Biochem. Biophys. 40: 346-351.
    • (1952) Arch. Biochem. Biophys. , vol.40 , pp. 346-351
    • Astrup, T.1    Mullertz, S.2
  • 17
    • 37049031217 scopus 로고    scopus 로고
    • Production of schizophyllan using Schizophyllum commune NRCM
    • Kumarl, M., Survase, S. A. and Singhal, R. S. 2008. Production of schizophyllan using Schizophyllum commune NRCM. Bioresour. Technol. 99: 1036-1043.
    • (2008) Bioresour. Technol. , vol.99 , pp. 1036-1043
    • Kumarl, M.1    Survase, S.A.2    Singhal, R.S.3
  • 18
    • 33645499292 scopus 로고    scopus 로고
    • Extracellular trypsin-like proteases produced by Cordyceps militaris
    • Hattori, M., Isomura, S., Yokoyama, E., Ujita, M. and Hara, A. 2005. Extracellular trypsin-like proteases produced by Cordyceps militaris. J. Biosci. Bioeng. 100: 631-636.
    • (2005) J. Biosci. Bioeng. , vol.100 , pp. 631-636
    • Hattori, M.1    Isomura, S.2    Yokoyama, E.3    Ujita, M.4    Hara, A.5
  • 19
    • 34250692159 scopus 로고    scopus 로고
    • Structure of fibrin: Impact on clot stability
    • Weisel, J. W. 2007. Structure of fibrin: impact on clot stability. J. Thromb. Haemost. 5 (Suppl. 1): 116-124.
    • (2007) J. Thromb. Haemost. , vol.5 , Issue.SUPPL. 1 , pp. 116-124
    • Weisel, J.W.1
  • 20
    • 0033253870 scopus 로고    scopus 로고
    • A fibrinolytic metalloprotease from the fruiting bodies of an edible mushroom, Armillariella mellea
    • Kim, J. H. and Kim, Y. S. 1999. A fibrinolytic metalloprotease from the fruiting bodies of an edible mushroom, Armillariella mellea. Biosci. Biotechnol. Biochem. 63: 2130-2136.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 2130-2136
    • Kim, J.H.1    Kim, Y.S.2
  • 23
    • 37849004068 scopus 로고    scopus 로고
    • A novel extracellular protease with fibrinolytic activity from the culture supernatant of Cordyceps sinensis: Purification and characterization
    • Li, H. P., Hu, Z., Yuan, J. L., Fan, H. D., Chen, W., Wang, S. J., Zheng, S. S., Zheng, Z. L. and Zou, G. L. 2007. A novel extracellular protease with fibrinolytic activity from the culture supernatant of Cordyceps sinensis: Purification and characterization. Phytother. Res. 21: 1234-1241.
    • (2007) Phytother. Res. , vol.21 , pp. 1234-1241
    • Li, H.P.1    Hu, Z.2    Yuan, J.L.3    Fan, H.D.4    Chen, W.5    Wang, S.J.6    Zheng, S.S.7    Zheng, Z.L.8    Zou, G.L.9
  • 26
    • 29144505132 scopus 로고    scopus 로고
    • Microbial fibrinolytic enzymes: An overview of source, production, properties, and thrombolytic activity in vivo
    • Peng, Y., Yang, X. and Zhang, Y. 2005. Microbial fibrinolytic enzymes: an overview of source, production, properties, and thrombolytic activity in vivo. Appl. Microbiol. Biotechnol. 69: 126-132.
    • (2005) Appl. Microbiol. Biotechnol. , vol.69 , pp. 126-132
    • Peng, Y.1    Yang, X.2    Zhang, Y.3
  • 27
    • 0033253870 scopus 로고    scopus 로고
    • A fibrinolytic metalloprotease from the fruiting bodies of an edible mushroom, Armillariella mellea
    • Kim, J. H. and Kim, Y. S. 1999. A fibrinolytic metalloprotease from the fruiting bodies of an edible mushroom, Armillariella mellea. Biosci. Biotechnol. Biochem. 63: 2130-2136.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 2130-2136
    • Kim, J.H.1    Kim, Y.S.2
  • 28
    • 0035259942 scopus 로고    scopus 로고
    • Characterization of a metalloenzyme from a wild mushroom, Tricholoma saponaceum
    • Kim, J. H. and Kim, Y. S. 2001. Characterization of a metalloenzyme from a wild mushroom, Tricholoma saponaceum. Biosci. Biotechnol. Biochem. 65: 356-362.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 356-362
    • Kim, J.H.1    Kim, Y.S.2
  • 29
    • 0030775983 scopus 로고    scopus 로고
    • Amino acid sequences of metalloendopeptidases specific for acyl-lysine bonds from Grifola frondosa and Pleurotus ostreatus fruiting bodies
    • Nonaka, T., Dohmae, N., Hashimoto, Y. and Takio, K. 1997. Amino acid sequences of metalloendopeptidases specific for acyl-lysine bonds from Grifola frondosa and Pleurotus ostreatus fruiting bodies. J. Biol. Chem. 272: 30032-30039.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30032-30039
    • Nonaka, T.1    Dohmae, N.2    Hashimoto, Y.3    Takio, K.4
  • 30
    • 0036631165 scopus 로고    scopus 로고
    • Divalent cations and the protein surface co-ordinate the intensity of human platelet adhesion and P-selectin surface expression
    • Whiss, P. A. and Andersson, R. G. 2002. Divalent cations and the protein surface co-ordinate the intensity of human platelet adhesion and P-selectin surface expression. Blood Coagul. Fibrinolysis 13: 407-416.
    • (2002) Blood Coagul. Fibrinolysis , vol.13 , pp. 407-416
    • Whiss, P.A.1    Andersson, R.G.2
  • 32
    • 0037161365 scopus 로고    scopus 로고
    • Comparative antithrombotic effects of magnesium sulfate and the platelet glycoprotein IIb/IIIa inhibitors tirofiban and eptifibatide in a canine model of stent thrombosis
    • DOI 10.1161/01.CIR.0000014612.88433.62
    • Rukshin, V., Shah, P. K., Cercek, B., Finkelstein, A., Tsang, V. and Kaul, S. 2002. Comparative antithrombotic effects of magnesium sulfate and the platelet glycoprotein IIb/IIIa inhibitors tirofiban and eptifibatide in a canine model of stent thrombosis. Circulation 105: 1970-1975. (Pubitemid 34437626)
    • (2002) Circulation , vol.105 , Issue.16 , pp. 1970-1975
    • Rukshin, V.1    Shah, P.K.2    Cercek, B.3    Finkelstein, A.4    Tsang, V.5    Kaul, S.6
  • 35
    • 0034968590 scopus 로고    scopus 로고
    • Intravenous magnesium does not influence the activity of the coagulation cascade
    • Ravn, H. B., Lassen, J. F., Bergenhem, N. and Kristensen, A. T. 2001. Intravenous magnesium does not influence the activity of the coagulation cascade. Blood Coagul. Fibrinolysis 12: 223-228.
    • (2001) Blood Coagul. Fibrinolysis , vol.12 , pp. 223-228
    • Ravn, H.B.1    Lassen, J.F.2    Bergenhem, N.3    Kristensen, A.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.