메뉴 건너뛰기




Volumn 19, Issue 3, 2014, Pages 3552-3569

Protein-rich fraction of cnidoscolus urens (L.) arthur leaves: Enzymatic characterization and procoagulant and fibrinogenolytic activities

Author keywords

Cnidoscolus urens; Cysteine proteases; Enzymatic characterization; Euphorbiaceae; Fibrin(ogen)olytic; Procoagulant

Indexed keywords

COAGULATING AGENT; FIBRINOGEN; FIBRINOLYTIC AGENT; METAL; PEPTIDE HYDROLASE; PLANT EXTRACT;

EID: 84896967507     PISSN: None     EISSN: 14203049     Source Type: Journal    
DOI: 10.3390/molecules19033552     Document Type: Article
Times cited : (17)

References (34)
  • 1
    • 84861535846 scopus 로고
    • A novel serine protease with human fibrino(geno)lytic activities from artocarpus heterophyllus latex
    • Siritapetawee, J.; Thumanu, K.; Sojikul, P.; Thammasirirak, S. A novel serine protease with human fibrino(geno)lytic activities from Artocarpus heterophyllus latex. Biochim. Biophys. Acta 2012, 1824, 907-912.
    • (1824) Biochim. Biophys. Acta , vol.2012 , pp. 907-912
    • Siritapetawee, J.1    Thumanu, K.2    Sojikul, P.3    Thammasirirak, S.4
  • 3
    • 79953050811 scopus 로고    scopus 로고
    • A new fibrinolytic enzyme (55 kda) from allium tuberosum: Purification, characterization, and comparison
    • Chung, D.M.; Choi, N.S.; Chun, H.K.; Maeng, P.J.; Park, S.B.; Kim, S.H. A new fibrinolytic enzyme (55 kDa) from Allium tuberosum: Purification, characterization, and comparison. J. Med. Food. 2010, 13, 1532-1536.
    • (2010) J. Med. Food. , vol.13 , pp. 1532-1536
    • Chung, D.M.1    Choi, N.S.2    Chun, H.K.3    Maeng, P.J.4    Park, S.B.5    Kim, S.H.6
  • 4
    • 79957664302 scopus 로고    scopus 로고
    • Purification and characterization of a novel fibrinolytic enzyme from chive (allium tuberosum)
    • Chung, D.M.; Choi, N.S.; Maeng, P.; Chun, H.; Kim, S.H. Purification and characterization of a novel fibrinolytic enzyme from chive (Allium tuberosum). Food Sci. Biotechnol. 2010, 19, 697-702.
    • (2010) Food Sci. Biotechnol. , vol.19 , pp. 697-702
    • Chung, D.M.1    Choi, N.S.2    Maeng, P.3    Chun, H.4    Kim, S.H.5
  • 6
    • 33750495382 scopus 로고    scopus 로고
    • Purification and characterization of a 34-kda, heat stable glycoprotein from synadenium grantii latex: Action on human fibrinogen and fibrin clot
    • Rajesh, R.; Nataraju, A.; Gowda, C.D.R.; Frey, B.M.; Frey, F.J.; Vishwanath, B.S. Purification and characterization of a 34-kDa, heat stable glycoprotein from Synadenium grantii latex: Action on human fibrinogen and fibrin clot. Biochimie 2006, 88, 1313-1322.
    • (2006) Biochimie , vol.88 , pp. 1313-1322
    • Rajesh, R.1    Nataraju, A.2    Gowda, C.D.R.3    Frey, B.M.4    Frey, F.J.5    Vishwanath, B.S.6
  • 8
    • 34548639334 scopus 로고    scopus 로고
    • Comparative study on plant latex proteases and their involvement in hemostasis: A special emphasis on clot inducing and dissolving properties
    • Rajesh, R.; Shivaprasad, H.V.; Gowda, C.D.; Nataraju, A.; Dhananjaya, B.L.; Vishwanath, B.S. Comparative study on plant latex proteases and their involvement in hemostasis: A special emphasis on clot inducing and dissolving properties. Planta Med. 2007, 73, 1061-1067.
    • (2007) Planta Med. , vol.73 , pp. 1061-1067
    • Rajesh, R.1    Shivaprasad, H.V.2    Gowda, C.D.3    Nataraju, A.4    Dhananjaya, B.L.5    Vishwanath, B.S.6
  • 9
    • 0036456369 scopus 로고    scopus 로고
    • Activation and inactivation of human factor x by proteases derived from ficus carica
    • Richter, G.; Schwarz, H.P.; Dorner, F.; Turecek, P.L. Activation and inactivation of human factor X by proteases derived from Ficus carica. Br. J. Haematol. 2002, 119, 1042-1051.
    • (2002) Br. J. Haematol. , vol.119 , pp. 1042-1051
    • Richter, G.1    Schwarz, H.P.2    Dorner, F.3    Turecek, P.L.4
  • 10
    • 84865463093 scopus 로고    scopus 로고
    • Moringa oleifera lam.: Protease activity against blood coagulation cascade
    • Satish, A.; Sairam, S.; Ahmed, F.; Urooj, A. Moringa oleifera Lam.: Protease activity against blood coagulation cascade. Pharmacogn. Res. 2012, 4, 44-49.
    • (2012) Pharmacogn. Res. , vol.4 , pp. 44-49
    • Satish, A.1    Sairam, S.2    Ahmed, F.3    Urooj, A.4
  • 11
    • 76949094781 scopus 로고    scopus 로고
    • Pergularain e I"-A plant cysteine protease with thrombin-like activity from Pergularia extensa latex
    • Shivaprasad, H.V.; Rajaiah, R.; Frey, B.M.; Frey, F.J.; Vishwanath, B.S. "Pergularain e I"-A plant cysteine protease with thrombin-like activity from Pergularia extensa latex. Thromb. Res. 2010, 125, e100-e105.
    • (2010) Thromb. Res. , vol.125
    • Shivaprasad, H.V.1    Rajaiah, R.2    Frey, B.M.3    Frey, F.J.4    Vishwanath, B.S.5
  • 12
    • 84455178872 scopus 로고    scopus 로고
    • Purification and physicochemical characterization of a serine protease with fibrinolytic activity from latex of a medicinal herb euphorbia hirta
    • Patel, G.K.; Kawale, A.A.; Sharma, A.K. Purification and physicochemical characterization of a serine protease with fibrinolytic activity from latex of a medicinal herb Euphorbia hirta. Plant Physiol. Biochem. 2012, 52, 104-111.
    • (2012) Plant Physiol. Biochem. , vol.52 , pp. 104-111
    • Patel, G.K.1    Kawale, A.A.2    Sharma, A.K.3
  • 13
    • 34047116460 scopus 로고    scopus 로고
    • Re-examining hypotheses concerning the use and knowledge of medicinal plants: A study in the caatinga vegetation of ne brazil
    • Albuquerque, U.P.J. Re-examining hypotheses concerning the use and knowledge of medicinal plants: A study in the Caatinga vegetation of NE Brazil. Ethnobiol. Ethnomed. 2006, 2, 1-10.
    • (2006) Ethnobiol. Ethnomed. , vol.2 , pp. 1-10
    • Albuquerque, U.P.J.1
  • 20
    • 19544367786 scopus 로고    scopus 로고
    • Snake venom fibrin(ogen)olytic enzymes
    • Swenson, S.; Markland, F.S., Jr. Snake venom fibrin(ogen)olytic enzymes. Toxicon 2005, 45, 1021-1039.
    • (2005) Toxicon , vol.45 , pp. 1021-1039
    • Swenson, S.1    Markland Jr., F.S.2
  • 21
    • 0022189629 scopus 로고
    • The influence of snake venom enzymes on blood coagulation
    • Kornalik, F. The influence of snake venom enzymes on blood coagulation. Pharmacol. Ther. 1985, 29, 353-405.
    • (1985) Pharmacol. Ther. , vol.29 , pp. 353-405
    • Kornalik, F.1
  • 22
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • Markland, F.S. Snake venoms and the hemostatic system. Toxicon 1998, 36, 1749-1800.
    • (1998) Toxicon , vol.36 , pp. 1749-1800
    • Markland, F.S.1
  • 23
    • 51349143196 scopus 로고    scopus 로고
    • Cysteine protease (capparin) from capsules of caper (capparis spinosa)
    • Demir, Y.; Gungor, A.A.; Duran, E.D.; Demir, N. Cysteine protease (Capparin) from capsules of caper (Capparis spinosa). Food Technol. Biotechnol. 2008, 46, 286-291.
    • (2008) Food Technol. Biotechnol. , vol.46 , pp. 286-291
    • Demir, Y.1    Gungor, A.A.2    Duran, E.D.3    Demir, N.4
  • 24
    • 79952900207 scopus 로고    scopus 로고
    • Ginger rhizome as a potential source of milk coagulating cysteine protease
    • Hashim, M.M.; Mingsheng, D.; Iqbal, M.F.; Xiaohong, C. Ginger rhizome as a potential source of milk coagulating cysteine protease. Phytochemistry 2011, 72, 458-464.
    • (2011) Phytochemistry , vol.72 , pp. 458-464
    • Hashim, M.M.1    Mingsheng, D.2    Iqbal, M.F.3    Xiaohong, C.4
  • 25
    • 0037376207 scopus 로고    scopus 로고
    • Procerain a stable cysteine protease from the latex of calotropis procera
    • Kumar Dubey, V.; Jagannadham, M.V. Procerain, a stable cysteine protease from the latex of Calotropis Procera. Phytochem. 2003, 62, 1057-1071.
    • (2003) Phytochem. , vol.62 , pp. 1057-1071
    • Kumar Dubey, V.1    Jagannadham, M.V.2
  • 26
    • 0033572187 scopus 로고    scopus 로고
    • Microbial alkaline proteases: From a bioindustrial viewpoint
    • Kumar, C.G.; Takagi, H. Microbial alkaline proteases: From a bioindustrial viewpoint. Biotechnol. Adv. 1999, 17, 561-594.
    • (1999) Biotechnol. Adv. , vol.17 , pp. 561-594
    • Kumar, C.G.1    Takagi, H.2
  • 27
    • 0242522901 scopus 로고    scopus 로고
    • Characterization of a cysteine protease from wheat triticum aestivum (cv. Giza 164)
    • Fahmy, A.S.; Ali, A.A.; Mohamed, S.A. Characterization of a cysteine protease from wheat Triticum aestivum (cv. Giza 164). Bioresour. Technol. 2004, 91, 297-304.
    • (2004) Bioresour. Technol. , vol.91 , pp. 297-304
    • Fahmy, A.S.1    Ali, A.A.2    Mohamed, S.A.3
  • 29
    • 80051793537 scopus 로고    scopus 로고
    • Artocarpus integer leaf protease: Purification and characterisation
    • Siti Balqis, Z.; Rosma, A. Artocarpus integer leaf protease: Purification and characterisation. Food Chem. 2011, 129, 1523-1529.
    • (2011) Food Chem. , vol.129 , pp. 1523-1529
    • Siti Balqis, Z.1    Rosma, A.2
  • 30
    • 52649126793 scopus 로고    scopus 로고
    • Proteolytic digestive enzymes and peritrophic membranes during the development of plodia interpunctella (lepidoptera: Piralidae): Targets for the action of soybean trypsin inhibitor (sbti) and chitin-binding vicilin (evv)
    • Amorim, T.M.; Macedo, L.L.; Uchoa, A.F.; Oliveira, A.S.; Pitanga, J.C.; Macedo, F.P.; Santos, E.A.; de Sales, M.P. Proteolytic digestive enzymes and peritrophic membranes during the development of Plodia interpunctella (Lepidoptera: Piralidae): Targets for the action of soybean trypsin inhibitor (SBTI) and chitin-binding vicilin (EvV). J. Agric. Food. Chem. 2008, 56, 7738-7745.
    • (2008) J. Agric. Food. Chem. , vol.56 , pp. 7738-7745
    • Amorim, T.M.1    Macedo, L.L.2    Uchoa, A.F.3    Oliveira, A.S.4    Pitanga, J.C.5    Macedo, F.P.6    Santos, E.A.7    De Sales, M.P.8
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage t4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0032125173 scopus 로고    scopus 로고
    • Detection and characterization of metalloproteinases with gelatinolytic, fibronectinolytic and fibrinogenolytic activities in brown spider (loxosceles intermedia) venom
    • Feitosa, L.; Gremski, W.; Veiga, S.S.; Elias, M.C.Q.B.; Graner, E.; Mangili, O.C.; Brentani, R.R. Detection and characterization of metalloproteinases with gelatinolytic, fibronectinolytic and fibrinogenolytic activities in Brown spider (Loxosceles intermedia) venom. Toxicon 1998, 36, 1039-1051.
    • (1998) Toxicon , vol.36 , pp. 1039-1051
    • Feitosa, L.1    Gremski, W.2    Veiga, S.S.3    Elias, M.C.Q.B.4    Graner, E.5    Mangili, O.C.6    Brentani, R.R.7
  • 33
    • 0024372242 scopus 로고
    • Comparative study on coagulant, defibrinating, fibrinolytic and fibrinogenolytic activities of costa rican crotaline snake venoms and their neutralization by a polyvalent antivenom
    • Gené, J.; Roy, A.; Rojas, G.; Gutiérrez, J.; Cerdas, L. Comparative study on coagulant, defibrinating, fibrinolytic and fibrinogenolytic activities of Costa Rican crotaline snake venoms and their neutralization by a polyvalent antivenom. Toxicon 1989, 27, 841-848.
    • (1989) Toxicon , vol.27 , pp. 841-848
    • Gené, J.1    Roy, A.2    Rojas, G.3    Gutiérrez, J.4    Cerdas, L.5
  • 34
    • 0021241015 scopus 로고
    • 3 Isolation and biochemical characterization of hemorrhagic toxin f from the venom of crotalus atrox (western diamondback rattlesnake)
    • Nikai, T.; Mori, N.; Kishida, M.; Sugihara, H.; Tu, A.T. Isolation and biochemical characterization of hemorrhagic toxin f from the venom of Crotalus atrox (Western Diamondback Rattlesnake). Arch. Biochem. Biophys. 1984, 231, 309-319.
    • (1984) Arch. Biochem. Biophys. , vol.231 , pp. 309-319
    • Nikai, T.1    Mori, N.2    Kishida, M.3    Sugihara, H.4    Tu, A.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.