메뉴 건너뛰기




Volumn 103, Issue 1, 2014, Pages 50-60

Characterization, mechanism of anticoagulant action, and assessment of therapeutic potential of a fibrinolytic serine protease (Brevithrombolase) purified from Brevibacillus brevis strain FF02B

Author keywords

Anticoagulant; Brevibacillus brevis; Plasmin like fibrinolytic protease; Thrombin degradation; Thrombolytic drug

Indexed keywords

ANTICOAGULANT AGENT; ANTITHROMBIN III; BREVITHROMBOLASE; CASEIN; CHROMOGENIC SUBSTRATE; FIBRINOGEN; GLOBULIN; HEPARIN; HYDROLASE; PLASMIN; SERINE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; STREPTOKINASE; UNCLASSIFIED DRUG; WARFARIN; AMIDE; BLOOD CLOTTING FACTOR 10A; THROMBIN;

EID: 84903625161     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2014.04.002     Document Type: Article
Times cited : (35)

References (46)
  • 1
    • 84877751512 scopus 로고    scopus 로고
    • Thrombolytic, anticoagulant and antiplatelet activities of codiase, a bi-functional fibrinolytic enzyme from Codium fragile
    • J.H. Choi, K. Sapkota, S.E. Park, S. Kim, and S.J. Kim Thrombolytic, anticoagulant and antiplatelet activities of codiase, a bi-functional fibrinolytic enzyme from Codium fragile Biochimie 95 2013 1266 1277
    • (2013) Biochimie , vol.95 , pp. 1266-1277
    • Choi, J.H.1    Sapkota, K.2    Park, S.E.3    Kim, S.4    Kim, S.J.5
  • 2
    • 84899619667 scopus 로고    scopus 로고
    • Hypertension in developing countries
    • 10.1016/j.cjca.2014.02.020
    • K.B. Tibazarwa, and A.A. Damasceno Hypertension in developing countries Can. J. Cardiol. 2014 10.1016/j.cjca.2014.02.020
    • (2014) Can. J. Cardiol.
    • Tibazarwa, K.B.1    Damasceno, A.A.2
  • 3
    • 77949295517 scopus 로고    scopus 로고
    • Direct fibrinolytic agents: Biochemical attributes preclinical foundation and clinical potential
    • V.J. Marder, and V. Novokhatny Direct fibrinolytic agents: biochemical attributes preclinical foundation and clinical potential J. Thromb. Haemost. 8 2010 433 444
    • (2010) J. Thromb. Haemost. , vol.8 , pp. 433-444
    • Marder, V.J.1    Novokhatny, V.2
  • 5
    • 0029960565 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp strain CK 11-4 screened from Chungkook-Jang
    • W. Kim, K. Choi, Y. Kim, H. Park, J. Choi, Y. Lee, H. Oh, I. Kwon, and S. Lee Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from Chungkook-Jang Appl. Environ. Microbiol. 62 1996 2482 2488
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2482-2488
    • Kim, W.1    Choi, K.2    Kim, Y.3    Park, H.4    Choi, J.5    Lee, Y.6    Oh, H.7    Kwon, I.8    Lee, S.9
  • 6
    • 85044705645 scopus 로고    scopus 로고
    • Characterization of urokinase type plasminogen activator modified by phenylglyoxal
    • L.I. Mukhametova, R.B. AÄ-sina, and S.D. Varfolomeev Characterization of urokinase type plasminogen activator modified by phenylglyoxal Bioorg. Khim. 28 2001 308 314
    • (2001) Bioorg. Khim. , vol.28 , pp. 308-314
    • Mukhametova, L.I.1    Aä-Sina, R.B.2    Varfolomeev, S.D.3
  • 7
    • 84880511613 scopus 로고    scopus 로고
    • Activity assessment of microbial fibrinolytic enzymes
    • E. Kotb Activity assessment of microbial fibrinolytic enzymes Appl. Microbiol. Biotechnol. 97 2013 6647 6665
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 6647-6665
    • Kotb, E.1
  • 8
    • 17144382779 scopus 로고    scopus 로고
    • Bacillolysin MA, a novel bacterial metalloproteinase that produces angiostatin-like fragments from plasminogen and activates protease zymogens in the coagulation and fibrinolysis systems
    • R. Narasaki, H. Kuribayashi, K. Shimizu, D. Imamura, T. Sato, and K. Hasumi Bacillolysin MA, a novel bacterial metalloproteinase that produces angiostatin-like fragments from plasminogen and activates protease zymogens in the coagulation and fibrinolysis systems J. Biol. Chem. 280 2005 14278 14287
    • (2005) J. Biol. Chem. , vol.280 , pp. 14278-14287
    • Narasaki, R.1    Kuribayashi, H.2    Shimizu, K.3    Imamura, D.4    Sato, T.5    Hasumi, K.6
  • 9
    • 79957861025 scopus 로고    scopus 로고
    • A low molecular weight chymotrypsin-like novel fibrinolytic enzyme from Streptomyces sp. CS624
    • P. Mander, S.S. Cho, J.R. Simkhada, Y.H. Choi, and J.C. Yoo A low molecular weight chymotrypsin-like novel fibrinolytic enzyme from Streptomyces sp. CS624 Process Biochem. 46 2011 1449 1455
    • (2011) Process Biochem. , vol.46 , pp. 1449-1455
    • Mander, P.1    Cho, S.S.2    Simkhada, J.R.3    Choi, Y.H.4    Yoo, J.C.5
  • 10
    • 84860466299 scopus 로고    scopus 로고
    • Bafibrinase: A non-toxic, non-hemorrhagic, direct-acting fibrinolytic serine protease from Bacillus sp strain AS-S20-I exhibits in vivo anticoagulant activity and thrombolytic potency
    • A.K. Mukherjee, S.K. Rai, R. Thakur, P. Chattopadhyay, and S.K. Kar Bafibrinase: a non-toxic, non-hemorrhagic, direct-acting fibrinolytic serine protease from Bacillus sp. strain AS-S20-I exhibits in vivo anticoagulant activity and thrombolytic potency Biochimie 94 2012 1300 1308
    • (2012) Biochimie , vol.94 , pp. 1300-1308
    • Mukherjee, A.K.1    Rai, S.K.2    Thakur, R.3    Chattopadhyay, P.4    Kar, S.K.5
  • 11
    • 17844395238 scopus 로고    scopus 로고
    • Purification and characterization of a novel fibrinolytic enzyme from Rhizopus chinensis 12
    • L. Xiao Lan, D. Lian Xiang, L. Fu Ping, Z. Xi Qun, and X. Jing Purification and characterization of a novel fibrinolytic enzyme from Rhizopus chinensis 12 Appl. Microbiol. Biotechnol. 67 2005 209 214
    • (2005) Appl. Microbiol. Biotechnol. , vol.67 , pp. 209-214
    • Xiao Lan, L.1    Lian Xiang, D.2    Fu Ping, L.3    Xi Qun, Z.4    Jing, X.5
  • 12
    • 78149285759 scopus 로고    scopus 로고
    • Purification and characterization of a novel anticoagulant and fibrinolytic enzyme produced by endophytic bacterium Paenibacillus polymyxa EJS-3
    • F. Lu, Z. Lu, X. Bie, Z. Yao, Y. Wang, Y. Lu, and Y. Guo Purification and characterization of a novel anticoagulant and fibrinolytic enzyme produced by endophytic bacterium Paenibacillus polymyxa EJS-3 Thrombo. Res. 126 2010 e349 e355
    • (2010) Thrombo. Res. , vol.126
    • Lu, F.1    Lu, Z.2    Bie, X.3    Yao, Z.4    Wang, Y.5    Lu, Y.6    Guo, Y.7
  • 13
    • 76649133434 scopus 로고    scopus 로고
    • Characterisation of a detergent-stable alkaline protease from a novel thermophilic strain Paenibacillus tezpurensis sp nov AS-S24-II
    • S.K. Rai, J.K. Roy, and A.K. Mukherjee Characterisation of a detergent-stable alkaline protease from a novel thermophilic strain Paenibacillus tezpurensis sp. nov. AS-S24-II Appl. Microbiol. Biotechnol. 85 2010 1437 1450
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 1437-1450
    • Rai, S.K.1    Roy, J.K.2    Mukherjee, A.K.3
  • 14
    • 33845738420 scopus 로고    scopus 로고
    • Crude petroleum-oil biodegradation efficiency of Bacillus subtilis and Pseudomonas aeruginosa strains isolated from a petroleum-oil contaminated soil from North-East India
    • K. Das, and A.K. Mukherjee Crude petroleum-oil biodegradation efficiency of Bacillus subtilis and Pseudomonas aeruginosa strains isolated from a petroleum-oil contaminated soil from North-East India Bioresour. Technol. 98 2007 1339 1345
    • (2007) Bioresour. Technol. , vol.98 , pp. 1339-1345
    • Das, K.1    Mukherjee, A.K.2
  • 15
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0
    • K. Tamura, J. Dudley, M. Nei, and S. Kumar MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0 Mol. Biol. Evol. 24 2007 1596 1599
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 84875979932 scopus 로고    scopus 로고
    • Biochemical and pharmacological properties of a new thrombin-like serine protease (Russelobin) from the venom of Russell's Viper (Daboia russelii russelii) and assessment of its therapeutic potential
    • A.K. Mukherjee, and S.P. Mackessy Biochemical and pharmacological properties of a new thrombin-like serine protease (Russelobin) from the venom of Russell's Viper (Daboia russelii russelii) and assessment of its therapeutic potential Biochim. Biophys. Acta 1830 2013 3476 3488
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3476-3488
    • Mukherjee, A.K.1    Mackessy, S.P.2
  • 21
    • 84895744919 scopus 로고    scopus 로고
    • The pro-coagulant fibrinogenolytic serine protease isoenzymes purified from Daboia russelii russelii venom coagulate the blood through Factor v activation: Role of glycosylation on enzymatic activity
    • A.K. Mukherjee The pro-coagulant fibrinogenolytic serine protease isoenzymes purified from Daboia russelii russelii venom coagulate the blood through Factor V activation: role of glycosylation on enzymatic activity PLoS One 9 2014 e86823
    • (2014) PLoS One , vol.9 , pp. 86823
    • Mukherjee, A.K.1
  • 22
    • 84887351007 scopus 로고    scopus 로고
    • 2 purified from Daboia russelii russelii venom: Correlation with clinical manifestations in Russell's viper envenomed patients
    • 2 purified from Daboia russelii russelii venom: correlation with clinical manifestations in Russell's viper envenomed patients Toxicon 79 2013 291 300
    • (2013) Toxicon , vol.79 , pp. 291-300
    • Saikia, D.1    Majumdar, S.2    Mukherjee, A.K.3
  • 24
    • 84888175327 scopus 로고    scopus 로고
    • Characterization of a pro-angiogenic, novel peptide from Russell's viper (Daboia russelii russelii) venom
    • A.K. Mukherjee, S. Chatterjee, S. Majumder, D. Saikia, R. Thakur, and A. Chatterjee Characterization of a pro-angiogenic, novel peptide from Russell's viper (Daboia russelii russelii) venom Toxicon 77 2013 26 31
    • (2013) Toxicon , vol.77 , pp. 26-31
    • Mukherjee, A.K.1    Chatterjee, S.2    Majumder, S.3    Saikia, D.4    Thakur, R.5    Chatterjee, A.6
  • 25
    • 0032190365 scopus 로고    scopus 로고
    • Fibrin zymography: A direct analysis of fibrinolytic enzymes on gels
    • S.H. Kim, N.S. Choi, and W.Y. Lee Fibrin zymography: a direct analysis of fibrinolytic enzymes on gels Anal. Biochem. 263 1998 115
    • (1998) Anal. Biochem. , vol.263 , pp. 115
    • Kim, S.H.1    Choi, N.S.2    Lee, W.Y.3
  • 26
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • M. Dubois, K.A. Gilles, J.K. Hamilton, P.A.t. Rebers, and F. Smith Colorimetric method for determination of sugars and related substances Anal. Chem. 28 1956 350 356
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.T.4    Smith, F.5
  • 27
    • 40649109730 scopus 로고    scopus 로고
    • Characterization of a novel pro-coagulant metalloprotease (RVBCMP) possessing αβ-fibrinogenase and tissue haemorrhagic activity from venom of Daboia russelli russelli (Russell's viper): Evidence of distinct coagulant and haemorrhagic sites in RVBCMP
    • A.K. Mukherjee Characterization of a novel pro-coagulant metalloprotease (RVBCMP) possessing αβ-fibrinogenase and tissue haemorrhagic activity from venom of Daboia russelli russelli (Russell's viper): evidence of distinct coagulant and haemorrhagic sites in RVBCMP Toxicon 51 2008 923 933
    • (2008) Toxicon , vol.51 , pp. 923-933
    • Mukherjee, A.K.1
  • 29
    • 34548499560 scopus 로고    scopus 로고
    • Pharmacokinetic comparisons of tail-bleeding with cannula-or retro-orbital bleeding techniques in rats using six marketed drugs
    • Y.H. Hui, N.H. Huang, L. Ebbert, H. Bina, A. Chiang, C. Maples, M. Pritt, T. Kern, and N. Patel Pharmacokinetic comparisons of tail-bleeding with cannula-or retro-orbital bleeding techniques in rats using six marketed drugs J. Pharmacol. Toxicol 56 2007 256 264
    • (2007) J. Pharmacol. Toxicol , vol.56 , pp. 256-264
    • Hui, Y.H.1    Huang, N.H.2    Ebbert, L.3    Bina, H.4    Chiang, A.5    Maples, C.6    Pritt, M.7    Kern, T.8    Patel, N.9
  • 30
    • 79551489756 scopus 로고    scopus 로고
    • A statistical approach for the enhanced production of alkaline protease showing fibrinolytic activity from a newly isolated Gram-negative Bacillus sp strain AS-S20-I
    • A.K. Mukherjee, and S.K. Rai A statistical approach for the enhanced production of alkaline protease showing fibrinolytic activity from a newly isolated Gram-negative Bacillus sp. strain AS-S20-I N Biotechnol. 28 2011 182 189
    • (2011) N Biotechnol. , vol.28 , pp. 182-189
    • Mukherjee, A.K.1    Rai, S.K.2
  • 31
    • 0141717707 scopus 로고    scopus 로고
    • Jerdonase, a novel serine protease with kinin-releasing and fibrinogenolytic activity from Trimeresurus jerdonii venom
    • J.I.A. Yong Hong, J.I.N. Yang, L. Qiu Min, L.I. Dong Sheng, W. Wan Yu, and X. Yu Liang Jerdonase, a novel serine protease with kinin-releasing and fibrinogenolytic activity from Trimeresurus jerdonii venom Acta Biochem. 35 2003 689 694
    • (2003) Acta Biochem. , vol.35 , pp. 689-694
    • Yong Hong, J.I.A.1    Yang, J.I.N.2    Qiu Min, L.3    Dong Sheng, L.I.4    Wan Yu, W.5    Yu Liang, X.6
  • 32
    • 0021344451 scopus 로고
    • The subtilisin e gene of Bacillus subtilis is transcribed from a sigma 37 promoter in vivo
    • S.L. Wong, C.W. Price, D.S. Goldfarb, and R.H. DoI The subtilisin E gene of Bacillus subtilis is transcribed from a sigma 37 promoter in vivo Proc. Natl. Acad. Sci. 81 1984 1184 1188
    • (1984) Proc. Natl. Acad. Sci. , vol.81 , pp. 1184-1188
    • Wong, S.L.1    Price, C.W.2    Goldfarb, D.S.3    Doi, R.H.4
  • 33
    • 79953653240 scopus 로고    scopus 로고
    • Assignment of PolyProline II conformation and analysis of sequence structure relationship
    • Y. Mansiaux, A.P. Joseph, J.C. Gelly, and A.G. de Brevern Assignment of PolyProline II conformation and analysis of sequence structure relationship PLoS One 6 2011 e18401
    • (2011) PLoS One , vol.6 , pp. 18401
    • Mansiaux, Y.1    Joseph, A.P.2    Gelly, J.C.3    De Brevern, A.G.4
  • 35
    • 80052479968 scopus 로고    scopus 로고
    • Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes
    • A. Dell, A. Galadari, F. Sastre, and P. Hitchen Similarities and differences in the glycosylation mechanisms in prokaryotes and eukaryotes Int. J. Microbiol. 2010 2010 14
    • (2010) Int. J. Microbiol. , vol.2010 , pp. 14
    • Dell, A.1    Galadari, A.2    Sastre, F.3    Hitchen, P.4
  • 36
    • 0027741228 scopus 로고
    • Purification and characterization of a strong fibrinolytic enzyme (nattokinase) in the vegetable cheese natto, a popular soybean fermented food in Japan
    • M. Fujita, K. Nomura, K. Hong, Y. Ito, A. Asada, and S. Nishimuro Purification and characterization of a strong fibrinolytic enzyme (nattokinase) in the vegetable cheese natto, a popular soybean fermented food in Japan Biochem. Biophys. Res. Commun. 197 1993 1340 1347
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 1340-1347
    • Fujita, M.1    Nomura, K.2    Hong, K.3    Ito, Y.4    Asada, A.5    Nishimuro, S.6
  • 39
    • 13644263327 scopus 로고    scopus 로고
    • The production of recombinant APRP, an alkaline protease derived from Bacillus pumilus TYO-67, by in vitro refolding of pro-enzyme fixed on a solid surface
    • M. Takahashi, T. Sekine, N. Kuba, S. Nakamori, M. Yasuda, and H. Takagi The production of recombinant APRP, an alkaline protease derived from Bacillus pumilus TYO-67, by in vitro refolding of pro-enzyme fixed on a solid surface J. Biochem. 136 2004 549 556
    • (2004) J. Biochem. , vol.136 , pp. 549-556
    • Takahashi, M.1    Sekine, T.2    Kuba, N.3    Nakamori, S.4    Yasuda, M.5    Takagi, H.6
  • 40
    • 0037229448 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food
    • Y. Peng, Q. Huang, R.H. Zhang, and Y.Z. Zhang Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food Comp. Biochem. Physio. B 134 2003 45 52
    • (2003) Comp. Biochem. Physio. B , vol.134 , pp. 45-52
    • Peng, Y.1    Huang, Q.2    Zhang, R.H.3    Zhang, Y.Z.4
  • 41
    • 33746315610 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic enzyme of Bacillus subtilis DC33, isolated from Chinese traditional Douchi
    • C.T. Wang, B.P. Ji, B. Li, R. Nout, P.L. Li, H. Ji, and L.F. Chen Purification and characterization of a fibrinolytic enzyme of Bacillus subtilis DC33, isolated from Chinese traditional Douchi J. Ind. Microbiol. Biotechnol 33 2006 750 758
    • (2006) J. Ind. Microbiol. Biotechnol , vol.33 , pp. 750-758
    • Wang, C.T.1    Ji, B.P.2    Li, B.3    Nout, R.4    Li, P.L.5    Ji, H.6    Chen, L.F.7
  • 42
    • 33645353328 scopus 로고    scopus 로고
    • Structure and interaction modes of thrombin
    • W. Bode Structure and interaction modes of thrombin Blood Cells Mol. Dis. 36 2006 122 130
    • (2006) Blood Cells Mol. Dis. , vol.36 , pp. 122-130
    • Bode, W.1
  • 43
    • 0028785452 scopus 로고
    • Heparin: Mechanism of action, pharmacokinetics, dosing considerations, monitoring, efficacy, and safety
    • J. Hirsh, R. Raschke, T.E. Warkentin, J.E. Dalen, D. Deykin, and L. Poller Heparin: mechanism of action, pharmacokinetics, dosing considerations, monitoring, efficacy, and safety Chest J 108 1995 258S 275S
    • (1995) Chest J , vol.108
    • Hirsh, J.1    Raschke, R.2    Warkentin, T.E.3    Dalen, J.E.4    Deykin, D.5    Poller, L.6
  • 44
    • 0035128503 scopus 로고    scopus 로고
    • Oral anticoagulants: Mechanism of action, clinical effectiveness, and optimal therapeutic range
    • J. Hirsh, J.E. Dalen, D.R. Anderson, L. Poller, H. Bussey, J. Ansell, and D. Deykin Oral anticoagulants: mechanism of action, clinical effectiveness, and optimal therapeutic range Chest. J. 119 2001 8S 21S
    • (2001) Chest. J. , vol.119
    • Hirsh, J.1    Dalen, J.E.2    Anderson, D.R.3    Poller, L.4    Bussey, H.5    Ansell, J.6    Deykin, D.7
  • 45
    • 76449108492 scopus 로고    scopus 로고
    • Pharmacotherapy: Intracoronary streptokinase in acute myocardial infarction
    • P.W. Armstrong Pharmacotherapy: Intracoronary streptokinase in acute myocardial infarction Nat. Rev. Cardiol. 7 2013 67 69
    • (2013) Nat. Rev. Cardiol. , vol.7 , pp. 67-69
    • Armstrong, P.W.1
  • 46
    • 77957984928 scopus 로고    scopus 로고
    • Thrombolysis with plasmin implications for stroke treatment
    • V.J. Marder, R. Jahan, T. Gruber, A. Goyal, and V. Arora Thrombolysis with plasmin implications for stroke treatment Stroke 41 2010 S45 S49
    • (2010) Stroke , vol.41
    • Marder, V.J.1    Jahan, R.2    Gruber, T.3    Goyal, A.4    Arora, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.