메뉴 건너뛰기




Volumn 97, Issue 15, 2013, Pages 6647-6665

Activity assessment of microbial fibrinolytic enzymes

Author keywords

Esterolytic assays; Euglobulin clot lysis time; Fibrin plate method; Fibrinolytic activity; Fluorimetric assays; Thrombolysis

Indexed keywords

EUGLOBULIN CLOT LYSIS TIME; FIBRIN PLATE METHOD; FIBRINOLYTIC ACTIVITY; FLUORIMETRIC ASSAYS; THROMBOLYSIS;

EID: 84880511613     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-013-5052-1     Document Type: Review
Times cited : (77)

References (182)
  • 2
    • 0021422260 scopus 로고
    • Purification and some properties of pure Cochliobolus lunatus fibrinolytic enzyme
    • 18553333 1:CAS:528:DyaL2cXktF2msbw%3D 10.1002/bit.260260502
    • Abdel-Fattah AF, Ismail AS (1984) Purification and some properties of pure Cochliobolus lunatus fibrinolytic enzyme. Biotechnol Bioeng 26(5):407-411
    • (1984) Biotechnol Bioeng , vol.26 , Issue.5 , pp. 407-411
    • Abdel-Fattah, A.F.1    Ismail, A.S.2
  • 3
    • 70349761446 scopus 로고    scopus 로고
    • Fibrinolytic enzymes from a newly isolated marine bacterium Bacillus subtilis A26 characterization and statistical media optimization
    • 19898547 1:CAS:528:DC%2BD1MXht1ant7nK 10.1139/W09-057
    • Agrebi R, Haddar A, Hajji M, Frikha F, Manni L, Jellouli K, Nasri M (2009) Fibrinolytic enzymes from a newly isolated marine bacterium Bacillus subtilis A26 characterization and statistical media optimization. Can J Microbiol 55(9):1049-1061
    • (2009) Can J Microbiol , vol.55 , Issue.9 , pp. 1049-1061
    • Agrebi, R.1    Haddar, A.2    Hajji, M.3    Frikha, F.4    Manni, L.5    Jellouli, K.6    Nasri, M.7
  • 4
    • 1642411066 scopus 로고    scopus 로고
    • Purification and characterization of a serine protease with fibrinolytic activity from the dung beetles, Catharsius molossus
    • 15041280 1:CAS:528:DC%2BD2cXisVaqu7w%3D 10.1016/j.thromres.2004.01.005
    • Ahn MY, Hahn BS, Ryu KS (2003) Purification and characterization of a serine protease with fibrinolytic activity from the dung beetles, Catharsius molossus. Thromb Res 112:339-347
    • (2003) Thromb Res , vol.112 , pp. 339-347
    • Ahn, M.Y.1    Hahn, B.S.2    Ryu, K.S.3
  • 5
    • 50449151040 scopus 로고
    • The fibrin plate method for estimating fibrinolytic activity
    • 12997222 1:CAS:528:DyaG3sXms1yj 10.1016/0003-9861(52)90121-5
    • Astrup T, Mullertz S (1952) The fibrin plate method for estimating fibrinolytic activity. Arch Biochem 40:346
    • (1952) Arch Biochem , vol.40 , pp. 346
    • Astrup, T.1    Mullertz, S.2
  • 6
    • 0036037356 scopus 로고    scopus 로고
    • Unfolding and aggregation during the thermal denaturation of streptokinase
    • 12180989 1:CAS:528:DC%2BD38XmslygtLo%3D 10.1046/j.1432-1033.2002.03107.x
    • Azuaga AI, Dobson CM, Mateo PL, Conejero-Lara F (2002) Unfolding and aggregation during the thermal denaturation of streptokinase. Eur J Biochem 269:4121-4133
    • (2002) Eur J Biochem , vol.269 , pp. 4121-4133
    • Azuaga, A.I.1    Dobson, C.M.2    Mateo, P.L.3    Conejero-Lara, F.4
  • 7
    • 0002873247 scopus 로고
    • Proteolytic enzymes: Aspartic and metallopeptidases
    • 10.1016/0076-6879(95)48015-3
    • Barett AJ (1995) Proteolytic enzymes: aspartic and metallopeptidases. Methods Enzymol 248:183
    • (1995) Methods Enzymol , vol.248 , pp. 183
    • Barett, A.J.1
  • 8
    • 0018897168 scopus 로고
    • Plasma urokinase levels measured by chromogenic assay after infusions of tissue culture or urinary source material
    • 1:CAS:528:DyaL3cXlsVamsb0%3D 10.1016/0049-3848(80)90338-2
    • Barlow GH, Marder VJ (1980) Plasma urokinase levels measured by chromogenic assay after infusions of tissue culture or urinary source material. Throm Res 18:431-437
    • (1980) Throm Res , vol.18 , pp. 431-437
    • Barlow, G.H.1    Marder, V.J.2
  • 9
    • 0013890311 scopus 로고
    • Dyed fibrin plate assay of fibrinolysis
    • 5946561 1:CAS:528:DyaF28XnvVSqsQ%3D%3D 10.1139/y66-028
    • Barta G (1966) Dyed fibrin plate assay of fibrinolysis. Can J Physiol Pharmacol 44(2):233-240
    • (1966) Can J Physiol Pharmacol , vol.44 , Issue.2 , pp. 233-240
    • Barta, G.1
  • 10
    • 27644518525 scopus 로고    scopus 로고
    • Isolation, purification and resolution of the extracellular proteinase complex of Aspergillus ochraceus 513 with fibrinolytic and anticoagulant activities
    • 1:CAS:528:DC%2BD3MXotFGrsro%3D 10.1023/A:1012343718772
    • Batomunkueva BP, Egorov NS (2001) Isolation, purification and resolution of the extracellular proteinase complex of Aspergillus ochraceus 513 with fibrinolytic and anticoagulant activities. Microbiology 70(5):519-522
    • (2001) Microbiology , vol.70 , Issue.5 , pp. 519-522
    • Batomunkueva, B.P.1    Egorov, N.S.2
  • 11
    • 0035073044 scopus 로고    scopus 로고
    • Multidomain structure of a recombinant streptokinase. A differential scanning calorimetry study
    • 11330353 1:CAS:528:DC%2BD3MXislWms7w%3D 10.1023/A:1011044718840
    • Beldarrain A, Lopez-Lacomba JL, Kutyshenko VP, Serrano R, Cortijo M (2001) Multidomain structure of a recombinant streptokinase. A differential scanning calorimetry study. J Protein Chem 20:9-17
    • (2001) J Protein Chem , vol.20 , pp. 9-17
    • Beldarrain, A.1    Lopez-Lacomba, J.L.2    Kutyshenko, V.P.3    Serrano, R.4    Cortijo, M.5
  • 12
    • 0016169903 scopus 로고
    • A sensitive fluorometric assay for plasminogen, plasmin and streptokinase
    • 4277983 1:CAS:528:DyaE2MXht1OktA%3D%3D 10.1016/0003-2697(74)90346-7
    • Bell PH, Dziobkowski CT, Englert ME (1974) A sensitive fluorometric assay for plasminogen, plasmin and streptokinase. Anal Biochem 61:200-208
    • (1974) Anal Biochem , vol.61 , pp. 200-208
    • Bell, P.H.1    Dziobkowski, C.T.2    Englert, M.E.3
  • 13
    • 84990407112 scopus 로고
    • Fibrinolysis as related to the urea solubility of fibrin
    • 1:CAS:528:DyaF3MXns1Gjsg%3D%3D
    • Bickford AF Jr, Sokolow M (1961) Fibrinolysis as related to the urea solubility of fibrin. Thrombos Diathes haemorrh (Stuttg) 5:480
    • (1961) Thrombos Diathes Haemorrh (Stuttg) , vol.5 , pp. 480
    • Bickford, Jr.A.F.1    Sokolow, M.2
  • 15
    • 73649152497 scopus 로고
    • The effectiveness of activators in clot lysis, with special reference to fibrinolytic therapy: A new method for determination of preformed clot lysis
    • Blix S (1962) The effectiveness of activators in clot lysis, with special reference to fibrinolytic therapy: a new method for determination of preformed clot lysis. Acta Med Scand 172:386
    • (1962) Acta Med Scand , vol.172 , pp. 386
    • Blix, S.1
  • 16
    • 0029844320 scopus 로고    scopus 로고
    • The future of thrombolysis in the treatment of acute myocardial infarction
    • 11824005 10.1093/eurheartj/17.suppl-E.55
    • Bode C, Runge M, Smalling RW (1996) The future of thrombolysis in the treatment of acute myocardial infarction. Eur Heart J 17:55-60
    • (1996) Eur Heart J , vol.17 , pp. 55-60
    • Bode, C.1    Runge, M.2    Smalling, R.W.3
  • 17
    • 0035854772 scopus 로고    scopus 로고
    • Streptokinase triggers conformational activation of plasminogen through specific interactions of the amino-terminal sequence and stabilizes the active zymogen conformation
    • 11369771 1:CAS:528:DC%2BD3MXlsVKnsrY%3D 10.1074/jbc.M101966200
    • Boxrud PD, Verhamme IMA, Fay WP, Bock PE (2001) Streptokinase triggers conformational activation of plasminogen through specific interactions of the amino-terminal sequence and stabilizes the active zymogen conformation. J Biol Chem 276:26084-26089
    • (2001) J Biol Chem , vol.276 , pp. 26084-26089
    • Boxrud, P.D.1    Verhamme, I.M.A.2    Fay, W.P.3    Bock, P.E.4
  • 18
    • 0016237609 scopus 로고
    • A characterization of native streptokinase and altered streptokinase isolated from a human plasminogen activator complex
    • 4857058 1:CAS:528:DyaE2cXksF2rtLY%3D 10.1021/bi00707a010
    • Brockway WJ, Castellino FJ (1974) A characterization of native streptokinase and altered streptokinase isolated from a human plasminogen activator complex. Biochemistry 13:2063-2070
    • (1974) Biochemistry , vol.13 , pp. 2063-2070
    • Brockway, W.J.1    Castellino, F.J.2
  • 19
    • 84961036043 scopus 로고
    • The effect of citrate on euglobulin methods of estimating fibrinolytic activity
    • 13575554 1:CAS:528:DyaG1MXitlOrug%3D%3D 10.1136/jcp.11.5.403
    • Buckell M (1958) The effect of citrate on euglobulin methods of estimating fibrinolytic activity. J Clin Path 11:403
    • (1958) J Clin Path , vol.11 , pp. 403
    • Buckell, M.1
  • 20
    • 0015975933 scopus 로고
    • The plasminogen activator of vampire bat saliva
    • 4204546 1:STN:280:DyaE2c%2Fpt1SgsA%3D%3D
    • Cartwright T (1974) The plasminogen activator of vampire bat saliva. Blood 43:317-326
    • (1974) Blood , vol.43 , pp. 317-326
    • Cartwright, T.1
  • 21
    • 77955476618 scopus 로고    scopus 로고
    • Biochemical and enzymatic properties of a fibrinolytic enzyme from Pleorotus eryngii cultivated under solid-state conditions using corn cob
    • 20413306 1:CAS:528:DC%2BC3cXlvFWhsb0%3D 10.1016/j.biortech.2010.02.048
    • Cha WS, Park SS, Kim SJ, Choi D (2010) Biochemical and enzymatic properties of a fibrinolytic enzyme from Pleorotus eryngii cultivated under solid-state conditions using corn cob. Bioresour Technol 101:6475-6481
    • (2010) Bioresour Technol , vol.101 , pp. 6475-6481
    • Cha, W.S.1    Park, S.S.2    Kim, S.J.3    Choi, D.4
  • 22
    • 0342666058 scopus 로고
    • The fibrinolytic potential as a simple measure of spontaneous fibrinolysis
    • 13877892 1:STN:280:DyaF38%2FhvFWrtg%3D%3D 10.1136/jcp.15.3.228
    • Chakrabarti R, Fearnley GR (1962) The fibrinolytic potential as a simple measure of spontaneous fibrinolysis. J Clin Path 15:228
    • (1962) J Clin Path , vol.15 , pp. 228
    • Chakrabarti, R.1    Fearnley, G.R.2
  • 23
    • 26444579348 scopus 로고    scopus 로고
    • Vibrio vulnificus secretes a broad-specificity metalloprotease capable of interfering with blood homeostasis through prothrombin activation and fibrinolysis
    • 16199560 1:CAS:528:DC%2BD2MXhtFantb%2FJ 10.1128/JB.187.20.6909-6916.2005
    • Chang AK, Kim HY, Park JE, Acharya P, Park IS, Yoon SM, You HJ, Hahm KS, Park JK, Lee JS (2005) Vibrio vulnificus secretes a broad-specificity metalloprotease capable of interfering with blood homeostasis through prothrombin activation and fibrinolysis. J Bacteriol 187(20):6909-6916
    • (2005) J Bacteriol , vol.187 , Issue.20 , pp. 6909-6916
    • Chang, A.K.1    Kim, H.Y.2    Park, J.E.3    Acharya, P.4    Park, I.S.5    Yoon, S.M.6    You, H.J.7    Hahm, K.S.8    Park, J.K.9    Lee, J.S.10
  • 24
    • 0033864203 scopus 로고    scopus 로고
    • Potent fibrinolytic enzyme from a mutant of Bacillus subtilis IMR-NK1
    • 10956093 1:CAS:528:DC%2BD3cXktlerurg%3D 10.1021/jf000020k
    • Chang CT, Fan MH, Kuo FC, Sung HY (2000) Potent fibrinolytic enzyme from a mutant of Bacillus subtilis IMR-NK1. J Agric Food Chem 48(8):3210-3216
    • (2000) J Agric Food Chem , vol.48 , Issue.8 , pp. 3210-3216
    • Chang, C.T.1    Fan, M.H.2    Kuo, F.C.3    Sung, H.Y.4
  • 25
    • 21644451024 scopus 로고    scopus 로고
    • Efficient system of artificial oil bodies for functional expression and purification of recombinant nattokinase in Escherichia coli
    • 15941319 1:CAS:528:DC%2BD2MXjslKlsL0%3D 10.1021/jf050264a
    • Chiang CJ, Chen HC, Chao Y, Tzen JTC (2005) Efficient system of artificial oil bodies for functional expression and purification of recombinant nattokinase in Escherichia coli. J Agric Food Chem 53(12):4799-4804
    • (2005) J Agric Food Chem , vol.53 , Issue.12 , pp. 4799-4804
    • Chiang, C.J.1    Chen, H.C.2    Chao, Y.3    Tzen, J.T.C.4
  • 26
    • 0034527436 scopus 로고    scopus 로고
    • Potent fibrinolytic enzyme from a thermophilic Streptomyces megasporus strain SD5
    • 11123546 1:CAS:528:DC%2BD3MXnsVGlug%3D%3D 10.1046/j.1365-2672.2000.00831. x
    • Chitte RR, Dey S (2000) Potent fibrinolytic enzyme from a thermophilic Streptomyces megasporus strain SD5. Lett Appl Microbiol 31(6):405-410
    • (2000) Lett Appl Microbiol , vol.31 , Issue.6 , pp. 405-410
    • Chitte, R.R.1    Dey, S.2
  • 27
    • 0036113618 scopus 로고    scopus 로고
    • Production of a fibrinolytic enzyme by thermophilic Streptomyces species
    • 1:CAS:528:DC%2BD38XkvVGlsbs%3D 10.1023/A:1015252607118
    • Chitte RR, Dey S (2002) Production of a fibrinolytic enzyme by thermophilic Streptomyces species. World J Microbiol Biotechnol 18(4):289-294
    • (2002) World J Microbiol Biotechnol , vol.18 , Issue.4 , pp. 289-294
    • Chitte, R.R.1    Dey, S.2
  • 28
    • 0042069504 scopus 로고    scopus 로고
    • Fibrinolytic and antithrombotic protease from Ganoderma lucidum
    • 1:CAS:528:DC%2BD3cXktVOkt7c%3D 10.2307/3761514
    • Choi HS, Sa YS (2000) Fibrinolytic and antithrombotic protease from Ganoderma lucidum. Mycologia 92:545-552
    • (2000) Mycologia , vol.92 , pp. 545-552
    • Choi, H.S.1    Sa, Y.S.2
  • 29
    • 0035320981 scopus 로고    scopus 로고
    • Fibrinolytic and antithrombotic protease from Spirodela polyrhiza
    • 11388453 1:CAS:528:DC%2BD3MXjsVagsL4%3D 10.1271/bbb.65.781
    • Choi HS, Sa YS (2001) Fibrinolytic and antithrombotic protease from Spirodela polyrhiza. Biosci Biotechnol Biochem 65:781-786
    • (2001) Biosci Biotechnol Biochem , vol.65 , pp. 781-786
    • Choi, H.S.1    Sa, Y.S.2
  • 30
    • 0031826325 scopus 로고    scopus 로고
    • Purification and partial characterization of a fibrinolytic protease in Pleurotus ostreatus
    • 1:CAS:528:DyaK1cXlsFart74%3D 10.2307/3761226
    • Choi HS, Shin PH (1998) Purification and partial characterization of a fibrinolytic protease in Pleurotus ostreatus. Mycologia 90(4):674-679
    • (1998) Mycologia , vol.90 , Issue.4 , pp. 674-679
    • Choi, H.S.1    Shin, P.H.2
  • 31
    • 3142640594 scopus 로고    scopus 로고
    • Cloning, expression, and fibrin(ogen)olytic properties of a subtilisin DJ-4 gene from Bacillus sp. DJ-4
    • 15251215 1:CAS:528:DC%2BD2cXls1ajtb8%3D 10.1111/j.1574-6968.2004.tb09665. x
    • Choi NS, Chang KT, Jae Maeng P, Kim SH (2004) Cloning, expression, and fibrin(ogen)olytic properties of a subtilisin DJ-4 gene from Bacillus sp. DJ-4. FEMS Microbiol Lett 236(2):325-331
    • (2004) FEMS Microbiol Lett , vol.236 , Issue.2 , pp. 325-331
    • Choi, N.S.1    Chang, K.T.2    Jae Maeng, P.3    Kim, S.H.4
  • 32
    • 77956195979 scopus 로고    scopus 로고
    • Expression and identification of a minor extracellular fibrinolytic enzyme (Vpr) from Bacillus subtilis KCTC 3014
    • 1:CAS:528:DC%2BC3cXosV2itb4%3D 10.1007/s12257-009-0191-z
    • Choi NS, Chung DM, Park CS, Ahn KH, Kim JS, Song JJ, Kim SH, Yoon BD, Kim MS (2010) Expression and identification of a minor extracellular fibrinolytic enzyme (Vpr) from Bacillus subtilis KCTC 3014. Biotechnol Bioprocess Eng 15(3):446-452
    • (2010) Biotechnol Bioprocess Eng , vol.15 , Issue.3 , pp. 446-452
    • Choi, N.S.1    Chung, D.M.2    Park, C.S.3    Ahn, K.H.4    Kim, J.S.5    Song, J.J.6    Kim, S.H.7    Yoon, B.D.8    Kim, M.S.9
  • 33
    • 61349184434 scopus 로고    scopus 로고
    • Purification and characterization of a novel thermoacid-stable fibrinolytic enzyme from Staphylococcus sp. strain AJ isolated from Korean salt-fermented Anchovy-joet
    • 19104859 10.1007/s10295-008-0512-9 1:CAS:528:DC%2BD1MXitlWrsLs%3D
    • Choi NS, Song JJ, Chung DM, Kim YJ, Maeng PJ, Kim SH (2008) Purification and characterization of a novel thermoacid-stable fibrinolytic enzyme from Staphylococcus sp. strain AJ isolated from Korean salt-fermented Anchovy-joet. J Ind Microbiol Biotechnol 36:417-426
    • (2008) J Ind Microbiol Biotechnol , vol.36 , pp. 417-426
    • Choi, N.S.1    Song, J.J.2    Chung, D.M.3    Kim, Y.J.4    Maeng, P.J.5    Kim, S.H.6
  • 34
    • 15044363063 scopus 로고    scopus 로고
    • Purification and characterization of a new peptidase, bacillopeptidase DJ-2, having fibrinolytic activity: Produced by Bacillus sp. DJ-2 from Doen-Jang
    • 1:CAS:528:DC%2BD2MXivFymt7w%3D
    • Choi NS, Yoo KH, Hahm JH, Yoon KS, Chang KT, Hyun BH, Maeng PJ, Kim SH (2005) Purification and characterization of a new peptidase, bacillopeptidase DJ-2, having fibrinolytic activity: produced by Bacillus sp. DJ-2 from Doen-Jang. J Microbiol Biotechnol 15(1):72-79
    • (2005) J Microbiol Biotechnol , vol.15 , Issue.1 , pp. 72-79
    • Choi, N.S.1    Yoo, K.H.2    Hahm, J.H.3    Yoon, K.S.4    Chang, K.T.5    Hyun, B.H.6    Maeng, P.J.7    Kim, S.H.8
  • 35
    • 0031794648 scopus 로고    scopus 로고
    • Engineered staphylokinase variants with reduced immunogenicity
    • 1:CAS:528:DyaK1cXnsFSkt7o%3D 10.1016/S0268-9499(98)80307-X
    • Collen D (1998a) Engineered staphylokinase variants with reduced immunogenicity. Fibrinol Proteol 12:59-65
    • (1998) Fibrinol Proteol , vol.12 , pp. 59-65
    • Collen, D.1
  • 36
    • 0031941584 scopus 로고    scopus 로고
    • Staphylokinase: A potent, uniquely fibrin-selective thrombolytic agent
    • 9500599 1:CAS:528:DyaK1cXhs1Gqu7k%3D 10.1038/nm0398-279
    • Collen D (1998b) Staphylokinase: a potent, uniquely fibrin-selective thrombolytic agent. Nat Med 4:279-284
    • (1998) Nat Med , vol.4 , pp. 279-284
    • Collen, D.1
  • 37
    • 5144220471 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator: A historical perspective and personal account
    • 15102005 1:CAS:528:DC%2BD2cXjslWntL0%3D 10.1111/j.1538-7933.2004.00645.x
    • Collen D, Lijnen HR (2004) Tissue-type plasminogen activator: a historical perspective and personal account. J Thromb Haemost 2(4):541-546
    • (2004) J Thromb Haemost , vol.2 , Issue.4 , pp. 541-546
    • Collen, D.1    Lijnen, H.R.2
  • 38
    • 0030448926 scopus 로고    scopus 로고
    • Thermal stability of the three domains of streptokinase studied by circular dichroism and nuclear magnetic resonance
    • 8976567 1:CAS:528:DyaK2sXjsFOi 10.1002/pro.5560051221
    • Conejero-Lara K, Parrado J, Azuaga AI, Smith RAG, Ponting CP, Dobson CM (1996) Thermal stability of the three domains of streptokinase studied by circular dichroism and nuclear magnetic resonance. Protein Sci 5:2583-2591
    • (1996) Protein Sci , vol.5 , pp. 2583-2591
    • Conejero-Lara, K.1    Parrado, J.2    Azuaga, A.I.3    Smith, R.A.G.4    Ponting, C.P.5    Dobson, C.M.6
  • 39
    • 41049092687 scopus 로고    scopus 로고
    • A novel fibrinolytic enzyme from Cordyceps militaris, a Chinese traditional medicinal mushroom
    • 1:CAS:528:DC%2BD1cXjsFWlt7w%3D 10.1007/s11274-007-9497-1
    • Cui L, Dong MS, Chen XH, Jiang M, Lv X, Yan G (2008) A novel fibrinolytic enzyme from Cordyceps militaris, a Chinese traditional medicinal mushroom. World J Microbiol Biotechnol 24:483-489
    • (2008) World J Microbiol Biotechnol , vol.24 , pp. 483-489
    • Cui, L.1    Dong, M.S.2    Chen, X.H.3    Jiang, M.4    Lv, X.5    Yan, G.6
  • 40
    • 77956456332 scopus 로고    scopus 로고
    • Medium optimization and immobilization of purified fibrinolytic URAK from Bacillus cereus NK1 on PHB nanoparticles
    • 1:CAS:528:DC%2BC3cXhtFGgsb3K 10.1016/j.enzmictec.2010.07.004
    • Deepak V, Ilangovan S, Sampathkumar MV, Victoria MJ, Pasha S, Pandian S, Gurunathan S (2010) Medium optimization and immobilization of purified fibrinolytic URAK from Bacillus cereus NK1 on PHB nanoparticles. Enzyme Microbial Technol 47(6):297-304
    • (2010) Enzyme Microbial Technol , vol.47 , Issue.6 , pp. 297-304
    • Deepak, V.1    Ilangovan, S.2    Sampathkumar, M.V.3    Victoria, M.J.4    Pasha, S.5    Pandian, S.6    Gurunathan, S.7
  • 41
    • 0036329424 scopus 로고    scopus 로고
    • Urokinase plasminogen activator and its inhibitor, PAI-1, as prognostic markers in breast cancer: From pilot to level 1 evidence studies
    • 12142372 1:CAS:528:DC%2BD38XlslKksb8%3D
    • Duffy MJ (2002) Urokinase plasminogen activator and its inhibitor, PAI-1, as prognostic markers in breast cancer: from pilot to level 1 evidence studies. Clin Chem 48(8):1194-1197
    • (2002) Clin Chem , vol.48 , Issue.8 , pp. 1194-1197
    • Duffy, M.J.1
  • 42
    • 0016958490 scopus 로고
    • Isolation and properties of the fibrinolytic enzyme from the Actinomyces thermovulgaris cultural broth
    • 12451 1:CAS:528:DyaE28XkvV2jtL8%3D
    • Egorov NS, Kochetov GA, Khaidarova NV (1976) Isolation and properties of the fibrinolytic enzyme from the Actinomyces thermovulgaris cultural broth. Mikrobiologiia 45:455-459
    • (1976) Mikrobiologiia , vol.45 , pp. 455-459
    • Egorov, N.S.1    Kochetov, G.A.2    Khaidarova, N.V.3
  • 43
    • 0021936949 scopus 로고
    • Streptomyces spheroides M8-2 strain-a producer of extracellular proteolytic enzyme possessing fibrinolytic and thrombolytic action
    • Egorov NS, Prianishnikova NI, Al-Nuri MA, Aslanian RR (1985) Streptomyces spheroides M8-2 strain-a producer of extracellular proteolytic enzyme possessing fibrinolytic and thrombolytic action. Naucn Dokl Vyss Sk Biol Nauki 1:77-81
    • (1985) Naucn Dokl Vyss Sk Biol Nauki , vol.1 , pp. 77-81
    • Egorov, N.S.1    Prianishnikova, N.I.2    Al-Nuri, M.A.3    Aslanian, R.R.4
  • 44
    • 0029123464 scopus 로고
    • Production and properties enzyme in solid state cultures of Fusarium pallidoroseum
    • 1:CAS:528:DyaK2MXosVSqt74%3D 10.1007/BF00127431
    • El-Aassar SA (1995) Production and properties enzyme in solid state cultures of Fusarium pallidoroseum. Biotechnol Lett 17(9):943-948
    • (1995) Biotechnol Lett , vol.17 , Issue.9 , pp. 943-948
    • El-Aassar, S.A.1
  • 45
    • 0025162433 scopus 로고
    • The biosynthesis of proteases with fibrinolytic activity in immobilized cultures of Penicillium chrysogenum H9
    • 1367445 1:CAS:528:DyaK3cXkt1aisLk%3D 10.1007/BF00170564
    • El-Aassar SA, El-Badry HM, Abdel-Fattah AF (1990) The biosynthesis of proteases with fibrinolytic activity in immobilized cultures of Penicillium chrysogenum H9. Appl Microbiol Biotechnol 33(1):26-30
    • (1990) Appl Microbiol Biotechnol , vol.33 , Issue.1 , pp. 26-30
    • El-Aassar, S.A.1    El-Badry, H.M.2    Abdel-Fattah, A.F.3
  • 46
    • 0000979904 scopus 로고
    • Evidence of a diurnal fibrinolytic rhythm; With a simple method of measuring natural fibrinolysis
    • 13489905 1:STN:280:DyaG1c%2Fjt1Knug%3D%3D
    • Fearnley GR, Balmforth G, Fearnley E (1957) Evidence of a diurnal fibrinolytic rhythm; with a simple method of measuring natural fibrinolysis. Clin Sci 16:645
    • (1957) Clin Sci , vol.16 , pp. 645
    • Fearnley, G.R.1    Balmforth, G.2    Fearnley, E.3
  • 48
    • 84880512366 scopus 로고
    • Proc. 7th Congr europ Soc Haemat. London part II
    • Flute PT (1960) Proc. 7th Congr europ Soc Haemat. London part II, p 894
    • (1960) , pp. 894
    • Flute, P.T.1
  • 49
    • 0030011657 scopus 로고    scopus 로고
    • Urokinase and non-urokinase fibrinolytic activity in protease-inhibitor- deprived plasma, assayed by a fibrin micro-plate method
    • 1:CAS:528:DyaK28XjsVOqsLc%3D 10.1016/0162-3109(95)00070-4
    • Fossum S, Hoem NO (1996) Urokinase and non-urokinase fibrinolytic activity in protease-inhibitor-deprived plasma, assayed by a fibrin micro-plate method. Immuno Pharmacol 32:119-121
    • (1996) Immuno Pharmacol , vol.32 , pp. 119-121
    • Fossum, S.1    Hoem, N.O.2
  • 50
    • 0027741228 scopus 로고
    • Purification and characterization of a strong fibrinolytic enzyme (nattokinase) in the vegetable cheese natto, a popular soybean fermented food in Japan
    • 8280151 1:CAS:528:DyaK2cXht1yhs7c%3D 10.1006/bbrc.1993.2624
    • Fujita M, Nomura K, Hong K, Ito Y, Asada A, Nishimuro S (1993) 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(3):1340-1347
    • (1993) Biochem Biophys Res Commun , vol.197 , Issue.3 , pp. 1340-1347
    • Fujita, M.1    Nomura, K.2    Hong, K.3    Ito, Y.4    Asada, A.5    Nishimuro, S.6
  • 51
    • 0014081538 scopus 로고
    • Effect of diluents on blood clot lysis
    • 5628854 1:CAS:528:DyaF2sXktlSgtL0%3D 10.1136/jcp.20.3.234
    • Gallimore MJ (1967) Effect of diluents on blood clot lysis. J Clin Path 20:234
    • (1967) J Clin Path , vol.20 , pp. 234
    • Gallimore, M.J.1
  • 52
    • 0029038699 scopus 로고
    • Complex transcriptional control of the streptokinase gene of Streptococcus equisimilis H46A
    • 7616967 1:CAS:528:DyaK2MXntFWgtrc%3D 10.1007/BF00290407
    • Gase K, Ellinger T, Malke H (1995) Complex transcriptional control of the streptokinase gene of Streptococcus equisimilis H46A. Mol Gen Genet 247:749-758
    • (1995) Mol Gen Genet , vol.247 , pp. 749-758
    • Gase, K.1    Ellinger, T.2    Malke, H.3
  • 53
    • 2642678145 scopus 로고
    • Staphylococcal coagulation and fibrinolysis
    • 18892126 1:STN:280:DyaH1c%2FjsFyksQ%3D%3D 10.1038/162732a0
    • Gerheim EB (1948) Staphylococcal coagulation and fibrinolysis. Nature 162:732
    • (1948) Nature , vol.162 , pp. 732
    • Gerheim, E.B.1
  • 54
    • 0017835538 scopus 로고
    • A rapid screening test for reduced fibrinolytic activity of plasma: Streptokinase activated lysis time
    • 627618 1:CAS:528:DyaE1cXhsVyms7w%3D 10.1136/jcp.31.1.54
    • Gidron E, Margalit R, Shalitin Y (1978) A rapid screening test for reduced fibrinolytic activity of plasma: streptokinase activated lysis time. J Clin Path 31:54-57
    • (1978) J Clin Path , vol.31 , pp. 54-57
    • Gidron, E.1    Margalit, R.2    Shalitin, Y.3
  • 55
    • 0008785944 scopus 로고
    • Protease and carotenogenesis in Blakeslea trispora
    • 1:CAS:528:DyaL38Xhtl2gu70%3D 10.1016/0031-9422(81)83076-2
    • Govind NS, Mehta B, Sharma M, Modi VV (1981) Protease and carotenogenesis in Blakeslea trispora. Phytochemistry 20:2483-2485
    • (1981) Phytochemistry , vol.20 , pp. 2483-2485
    • Govind, N.S.1    Mehta, B.2    Sharma, M.3    Modi, V.V.4
  • 56
    • 0029888893 scopus 로고    scopus 로고
    • Structural dissection and functional analysis of the complex promoter of the streptokinase gene from Streptococcus equisimilis H46A
    • 1:STN:280:DyaK28zps1yntw%3D%3D 10.1007/s004300050009
    • Grafe S, Ellinger T, Malke H (1996) Structural dissection and functional analysis of the complex promoter of the streptokinase gene from Streptococcus equisimilis H46A. Med Microbiol Immun 185:11-17
    • (1996) Med Microbiol Immun , vol.185 , pp. 11-17
    • Grafe, S.1    Ellinger, T.2    Malke, H.3
  • 57
    • 84858740730 scopus 로고    scopus 로고
    • Fibrinolysis and anticoagulant potential of a metallo protease produced by Bacillus subtilis K42
    • 22116275 1:CAS:528:DC%2BC38XksVOgu7w%3D 10.1007/s12038-011-9151-9
    • Hassanein WA, Kotb E, Awny NM, El-Zawahry YA (2011) Fibrinolysis and anticoagulant potential of a metallo protease produced by Bacillus subtilis K42. J Biosci 36:773-779
    • (2011) J Biosci , vol.36 , pp. 773-779
    • Hassanein, W.A.1    Kotb, E.2    Awny, N.M.3    El-Zawahry, Y.A.4
  • 59
    • 75949153911 scopus 로고
    • A standard clot method for the assay of plasminogen activators, anti-activators, and plasmin
    • 14149945 1:CAS:528:DyaF2MXmvVWgtw%3D%3D 10.1136/jcp.17.2.175
    • Hawkey CM, Stafford JL (1964) A standard clot method for the assay of plasminogen activators, anti-activators, and plasmin. J Clin Path 17:175
    • (1964) J Clin Path , vol.17 , pp. 175
    • Hawkey, C.M.1    Stafford, J.L.2
  • 60
    • 78651156831 scopus 로고
    • A method for assessing clot lysis
    • 14159468 1:CAS:528:DyaF2MXltlKqsg%3D%3D 10.1136/jcp.17.3.310
    • Howell M (1964) A method for assessing clot lysis. J Clin Path 17:310
    • (1964) J Clin Path , vol.17 , pp. 310
    • Howell, M.1
  • 61
    • 35348910280 scopus 로고    scopus 로고
    • Purification and characterization of a new fibrinolytic enzyme of Bacillus licheniformis KJ-31 isolated from Korean traditional Jeot-gal
    • 18062224 1:CAS:528:DC%2BD2sXht1Gks7bP
    • Hwang KJ, Choi KH, Kim MJ, Park CS, Cha J (2007) Purification and characterization of a new fibrinolytic enzyme of Bacillus licheniformis KJ-31 isolated from Korean traditional Jeot-gal. J Microbiol Biotechnol 17(9):1469-1476
    • (2007) J Microbiol Biotechnol , vol.17 , Issue.9 , pp. 1469-1476
    • Hwang, K.J.1    Choi, K.H.2    Kim, M.J.3    Park, C.S.4    Cha, J.5
  • 62
    • 0023722280 scopus 로고
    • In vitro processing of pro-subtilisin in Escherichia coli
    • 3047114 1:CAS:528:DyaL1cXmtVOnu7k%3D
    • Ikemura H, Inouye M (1988) In vitro processing of pro-subtilisin in Escherichia coli. J Biol Chem 263:12959-12963
    • (1988) J Biol Chem , vol.263 , pp. 12959-12963
    • Ikemura, H.1    Inouye, M.2
  • 63
    • 0020306559 scopus 로고
    • Complete amino acid sequence of streptokinase and its homology with serine proteases
    • 6760891 1:CAS:528:DyaL3sXit1Wm 10.1021/bi00269a001
    • Jackson KW, Tang J (1982) Complete amino acid sequence of streptokinase and its homology with serine proteases. Biochemistry 21:6620-6625
    • (1982) Biochemistry , vol.21 , pp. 6620-6625
    • Jackson, K.W.1    Tang, J.2
  • 64
    • 11844270541 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene encoding a fibrinolytic enzyme from Bacillus subtilis strain A1
    • 1:CAS:528:DC%2BD2cXpvV2qsrw%3D 10.1007/s11274-003-4514-5
    • Jeong YK, Kim JH, Gal SW, Kim JE, Park SS, Chung KT, Kim YH, Kim BW, Joo WH (2004) Molecular cloning and characterization of the gene encoding a fibrinolytic enzyme from Bacillus subtilis strain A1. World J Microbiol Biotechnol 20:711-717
    • (2004) World J Microbiol Biotechnol , vol.20 , pp. 711-717
    • Jeong, Y.K.1    Kim, J.H.2    Gal, S.W.3    Kim, J.E.4    Park, S.S.5    Chung, K.T.6    Kim, Y.H.7    Kim, B.W.8    Joo, W.H.9
  • 65
    • 0035024732 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a fibrinolytic enzyme from Bacillus subtilis BK-17
    • 1:CAS:528:DC%2BD3MXktlersbs%3D 10.1023/A:1016685411809
    • Jeong YK, Park JU, Baek H, Park SH, Kong IS, Kim DW, Joo WH (2001) Purification and biochemical characterization of a fibrinolytic enzyme from Bacillus subtilis BK-17. World J Microbiol Biotechnol 17:89-92
    • (2001) World J Microbiol Biotechnol , vol.17 , pp. 89-92
    • Jeong, Y.K.1    Park, J.U.2    Baek, H.3    Park, S.H.4    Kong, I.S.5    Kim, D.W.6    Joo, W.H.7
  • 67
    • 0021055664 scopus 로고
    • A study of the fibrin plate assay of fibrinolytic agents. Optimal conditions, reproducibility and precision
    • 1:CAS:528:DyaL2cXotFKgtQ%3D%3D
    • Jespersen J, Astrup T (1983) A study of the fibrin plate assay of fibrinolytic agents. Optimal conditions, reproducibility and precision. Haemost 13:301-315
    • (1983) Haemost , vol.13 , pp. 301-315
    • Jespersen, J.1    Astrup, T.2
  • 68
    • 0017100579 scopus 로고
    • Fluorometric microassay of plasminogen activators
    • 185962 1:CAS:528:DyaE28XlvVyiu7k%3D 10.1016/0003-9861(76)90183-1
    • Kessner A, Troll W (1976) Fluorometric microassay of plasminogen activators. Arch Biochem Biophys 176:411-416
    • (1976) Arch Biochem Biophys , vol.176 , pp. 411-416
    • Kessner, A.1    Troll, W.2
  • 69
    • 10644227920 scopus 로고    scopus 로고
    • Confirmation of Vpr as a fibrinolytic enzyme present in extracellular proteins of Bacillus subtilis
    • 15596354 1:CAS:528:DC%2BD2cXhtVKltbzM 10.1016/j.pep.2004.08.008
    • Kho CW, Park SG, Cho S, Lee DH, Myung PK, Park BC (2005) Confirmation of Vpr as a fibrinolytic enzyme present in extracellular proteins of Bacillus subtilis. Protein Expr Purif 39:1-7
    • (2005) Protein Expr Purif , vol.39 , pp. 1-7
    • Kho, C.W.1    Park, S.G.2    Cho, S.3    Lee, D.H.4    Myung, P.K.5    Park, B.C.6
  • 70
    • 0033938712 scopus 로고    scopus 로고
    • 48 region of streptokinase is important in binding to a substrate plasminogen
    • 10904106 1:CAS:528:DC%2BD3cXkvVyrsro%3D 10.1016/S0049-3848(00)00225-5
    • 48 region of streptokinase is important in binding to a substrate plasminogen. Thromb Res 99:93-98
    • (2000) Thromb Res , vol.99 , pp. 93-98
    • Kim, D.M.1    Lee, S.J.2    Kim, I.C.3    Kim, S.T.4    Byun, S.M.5
  • 71
    • 79960027341 scopus 로고    scopus 로고
    • Purification and characterization of a novel, highly potent fibrinolytic enzyme from Paecilomyces tenuipes
    • 1:CAS:528:DC%2BC3MXosFSqtb0%3D 10.1016/j.procbio.2011.04.005
    • Kim HC, Choi BS, Sapkota K, Kim S, Lee HJ, Yoo JC, Kim SJ (2011) Purification and characterization of a novel, highly potent fibrinolytic enzyme from Paecilomyces tenuipes. Process Biochem 46:1545-1553
    • (2011) Process Biochem , vol.46 , pp. 1545-1553
    • Kim, H.C.1    Choi, B.S.2    Sapkota, K.3    Kim, S.4    Lee, H.J.5    Yoo, J.C.6    Kim, S.J.7
  • 72
    • 0031442243 scopus 로고    scopus 로고
    • Purification and characterization of a novel fibrinolytic enzyme from Bacillus sp. KA38 originated from fermented fish
    • 1:CAS:528:DyaK2sXntlyjt7o%3D 10.1016/S0922-338X(97)89253-7
    • Kim HK, Kim GT, Kim DK, Choi WA, Park SH, Jeong YK, Kong IS (1997) Purification and characterization of a novel fibrinolytic enzyme from Bacillus sp. KA38 originated from fermented fish. J Ferment Bioeng 84(4):307-312
    • (1997) J Ferment Bioeng , vol.84 , Issue.4 , pp. 307-312
    • Kim, H.K.1    Kim, G.T.2    Kim, D.K.3    Choi, W.A.4    Park, S.H.5    Jeong, Y.K.6    Kong, I.S.7
  • 73
    • 33847755486 scopus 로고    scopus 로고
    • Identification of a fibrinolytic enzyme by Bacillus vallismortis and its potential as a bacteriolytic enzyme against Streptococcus mutans
    • 17308884 1:CAS:528:DC%2BD2sXis1eku7s%3D 10.1007/s10529-006-9284-3
    • Kim JB, Jung WH, Ryu JM, Lee YJ, Jung JK, Jang HW, Kim SW (2007) Identification of a fibrinolytic enzyme by Bacillus vallismortis and its potential as a bacteriolytic enzyme against Streptococcus mutans. Biotechnol Lett 29:605-610
    • (2007) Biotechnol Lett , vol.29 , pp. 605-610
    • Kim, J.B.1    Jung, W.H.2    Ryu, J.M.3    Lee, Y.J.4    Jung, J.K.5    Jang, H.W.6    Kim, S.W.7
  • 74
    • 0035259942 scopus 로고    scopus 로고
    • Characterization of a metalloenzyme from a wild mushroom, Tricholoma saponaceum
    • 1:CAS:528:DC%2BD3MXhslKgtLg%3D 10.1271/bbb.65.356
    • Kim JH, Kim YS (2001) Characterization of a metalloenzyme from a wild mushroom, Tricholoma saponaceum. Biosci Biotech Biochem 65(2):356-362
    • (2001) Biosci Biotech Biochem , vol.65 , Issue.2 , pp. 356-362
    • Kim, J.H.1    Kim, Y.S.2
  • 75
    • 0033253870 scopus 로고    scopus 로고
    • A fibrinolytic metalloprotease from the fruiting bodies of an edible mushroom, Armillariella mellea
    • 10664846 1:CAS:528:DC%2BD3cXlsFKltw%3D%3D 10.1271/bbb.63.2130
    • Kim JH, Kim YS (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
  • 77
    • 33646461272 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic subtilisin-like protease of Bacillus subtilis TP-6 from an Indonesian fermented soybean, Tempeh
    • 16470353 1:CAS:528:DC%2BD28XjvFSmsr8%3D 10.1007/s10295-006-0085-4
    • Kim SB, Lee DW, Cheigh CI, Choe EA, Lee SJ, Hong YH, Choi HJ, Pyun YR (2006) Purification and characterization of a fibrinolytic subtilisin-like protease of Bacillus subtilis TP-6 from an Indonesian fermented soybean, Tempeh. J Ind Microbiol Biotechnol 33:436-444
    • (2006) J Ind Microbiol Biotechnol , vol.33 , pp. 436-444
    • Kim, S.B.1    Lee, D.W.2    Cheigh, C.I.3    Choe, E.A.4    Lee, S.J.5    Hong, Y.H.6    Choi, H.J.7    Pyun, Y.R.8
  • 78
    • 0034251873 scopus 로고    scopus 로고
    • Purification and characterization of subtilisin DJ-4 secreted by Bacillus sp strain DJ-4 screened from Doen-Jang
    • 10993162 1:STN:280:DC%2BD3cvktlSksA%3D%3D 10.1271/bbb.64.1722
    • Kim SH, Choi NS (2000) Purification and characterization of subtilisin DJ-4 secreted by Bacillus sp strain DJ-4 screened from Doen-Jang. Biosci Biotechnol Biochem 64:1722-1725
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 1722-1725
    • Kim, S.H.1    Choi, N.S.2
  • 79
    • 0029960565 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from Chungkook-Jang
    • Kim W, Choi K, Kim Y, Park H, Choi J, Lee Y, Oh H, Kwon I, Lee S (1996) Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from Chungkook-Jang. Appl Environ Microbiol 62(7):1488-2482
    • (1996) Appl Environ Microbiol , vol.62 , Issue.7 , pp. 1488-2482
    • 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
  • 80
    • 0033956366 scopus 로고    scopus 로고
    • Short-term treatment of painful osteoarthritis of the knee with oral enzymes. A randomized, double-blind study versus diclofenac
    • 1:CAS:528:DC%2BD3cXpvFOltg%3D%3D 10.2165/00044011-200019010-00003
    • Klein G, Kullich W (2000) Short-term treatment of painful osteoarthritis of the knee with oral enzymes. A randomized, double-blind study versus diclofenac. Chem Drug Invest 19(1):15-23
    • (2000) Chem Drug Invest , vol.19 , Issue.1 , pp. 15-23
    • Klein, G.1    Kullich, W.2
  • 82
    • 0028889242 scopus 로고
    • High-level expression and secretion of streptokinase in Escherichia coli
    • 1:CAS:528:DyaK2MXptFGrtrY%3D 10.1007/BF00143093
    • Ko JH, Park DK, Kim IC, Lee SH, Byun SM (1995) High-level expression and secretion of streptokinase in Escherichia coli. Biotechnol Lett 17:1019-1024
    • (1995) Biotechnol Lett , vol.17 , pp. 1019-1024
    • Ko, J.H.1    Park, D.K.2    Kim, I.C.3    Lee, S.H.4    Byun, S.M.5
  • 83
    • 1242292321 scopus 로고    scopus 로고
    • Identification of two novel fibrinolytic enzymes from Bacillus subtilis QK02
    • 14984705 10.1016/j.cca.2003.11.008 1:CAS:528:DC%2BD2cXhsFWiurg%3D
    • Ko JH, Yan JP, Zhu L, Qi YP (2004) Identification of two novel fibrinolytic enzymes from Bacillus subtilis QK02. Comp Biochem Physiol C Toxicol Pharmacol 137:65-74
    • (2004) Comp Biochem Physiol C Toxicol Pharmacol , vol.137 , pp. 65-74
    • Ko, J.H.1    Yan, J.P.2    Zhu, L.3    Qi, Y.P.4
  • 85
    • 0027241627 scopus 로고
    • Highly sensitive chromogenic microplate assay for quantification of rat and human plasminógen
    • 8512067 1:CAS:528:DyaK3sXks1KiurY%3D 10.1006/abio.1993.1201
    • Kulseth MA, Helgeland LA (1993) Highly sensitive chromogenic microplate assay for quantification of rat and human plasminógen. Anal Biochem 210:314-317
    • (1993) Anal Biochem , vol.210 , pp. 314-317
    • Kulseth, M.A.1    Helgeland, L.A.2
  • 86
    • 29144462335 scopus 로고
    • The effect of natto possessing a high fibrinolytic activity in human plasma
    • 1:CAS:528:DyaK2cXjt1Wqtbg%3D
    • Kumada K, Onga T, Hoshino H (1994) The effect of natto possessing a high fibrinolytic activity in human plasma. Igaku To Seibutsugaku 128(3):117-119
    • (1994) Igaku to Seibutsugaku , vol.128 , Issue.3 , pp. 117-119
    • Kumada, K.1    Onga, T.2    Hoshino, H.3
  • 87
    • 1642336686 scopus 로고
    • On the solubility of fibrin clots
    • 17842715 1:STN:280:DC%2BC3czosVGhsQ%3D%3D 10.1126/science.108.2802.280
    • Laki K, Lorand L (1948) On the solubility of fibrin clots. Science 108:280
    • (1948) Science , vol.108 , pp. 280
    • Laki, K.1    Lorand, L.2
  • 88
    • 13244256422 scopus 로고
    • The estimation of fibrinolytic components by means of the lysis time method
    • 13615243 1:CAS:528:DyaF3cXksFWlsg%3D%3D 10.3109/00365515809051241
    • Lassen M (1958) The estimation of fibrinolytic components by means of the lysis time method. Scand J Clin Lab Invest 10:384-389
    • (1958) Scand J Clin Lab Invest , vol.10 , pp. 384-389
    • Lassen, M.1
  • 89
    • 84958690410 scopus 로고
    • Heat denaturation of plasminogen in the fibrin plate method
    • 13065142 1:CAS:528:DyaG3sXjsFWhsw%3D%3D 10.1111/j.1748-1716.1953.tb00951. x
    • Lassen N (1953) Heat denaturation of plasminogen in the fibrin plate method. Acta Physiol Scand 27:371
    • (1953) Acta Physiol Scand , vol.27 , pp. 371
    • Lassen, N.1
  • 90
    • 33646698183 scopus 로고    scopus 로고
    • Purification and characterization of two novel fibrinolytic proteases from mushroom, Fomitella raxinea
    • 1:CAS:528:DC%2BD2sXlsVSmsbs%3D
    • Lee JS, Bai HS, Park SS (2006) Purification and characterization of two novel fibrinolytic proteases from mushroom, Fomitella raxinea. J Microbiol Biotechnol 16:264-271
    • (2006) J Microbiol Biotechnol , vol.16 , pp. 264-271
    • Lee, J.S.1    Bai, H.S.2    Park, S.S.3
  • 91
    • 0035173791 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic enzyme from Bacillus sp. KDO-13 isolated from soybean paste
    • 1:CAS:528:DC%2BD3MXptVKqu7o%3D
    • Lee SK, Bae DH, Kwon TJ, Lee SB, Lee HH, Park JH, Heo S, Johnson MG (2001) Purification and characterization of a fibrinolytic enzyme from Bacillus sp. KDO-13 isolated from soybean paste. J Microbiol Biotechnol 11(5):845-852
    • (2001) J Microbiol Biotechnol , vol.11 , Issue.5 , pp. 845-852
    • Lee, S.K.1    Bae, D.H.2    Kwon, T.J.3    Lee, S.B.4    Lee, H.H.5    Park, J.H.6    Heo, S.7    Johnson, M.G.8
  • 93
    • 41049092687 scopus 로고    scopus 로고
    • A novel fibrinolytic enzyme from Cordyceps militaris, a Chinese traditional medicinal mushroom
    • 1:CAS:528:DC%2BD1cXjsFWlt7w%3D 10.1007/s11274-007-9497-1
    • Li C, Ming SD, Xiao HC, Mei J, Xin L, Guijun Y (2008) A novel fibrinolytic enzyme from Cordyceps militaris, a Chinese traditional medicinal mushroom. World J Microbiol Biotechnol 24:483-489
    • (2008) World J Microbiol Biotechnol , vol.24 , pp. 483-489
    • Li, C.1    Ming, S.D.2    Xiao, H.C.3    Mei, J.4    Xin, L.5    Guijun, Y.6
  • 94
    • 37849004068 scopus 로고    scopus 로고
    • A novel extracellular protease with fibrinolytic activity from the culture supernatant of Cordyceps sinensis: Purification and characterization
    • 17661328 1:CAS:528:DC%2BD1cXhvVCgsbY%3D 10.1002/ptr.2246
    • Li HP, Hu Z, Yuan JL, Fan HD, Chen W, Wang SJ, Zheng SS, Zheng ZL, Zou GL (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
  • 95
    • 0036396570 scopus 로고    scopus 로고
    • Molecular cloning and expression of nattokinase gene in Bacillus subtilis
    • 1:CAS:528:DC%2BD38XotlSqs7w%3D
    • Liu BY, Song HY (2002) Molecular cloning and expression of nattokinase gene in Bacillus subtilis. Acta Biochim Biophys Sin (Shanghai) 34(3):338-340
    • (2002) Acta Biochim Biophys Sin (Shanghai) , vol.34 , Issue.3 , pp. 338-340
    • Liu, B.Y.1    Song, H.Y.2
  • 96
    • 15744369257 scopus 로고    scopus 로고
    • Optimization of nutritional conditions for nattokinase production by Bacillus natto NLSSE using statistical experimental methods
    • 1:CAS:528:DC%2BD2MXis1KisL4%3D 10.1016/j.procbio.2004.12.025
    • Liu JG, Xing JM, Chang TS, Ma ZY, Liu HZ (2005) Optimization of nutritional conditions for nattokinase production by Bacillus natto NLSSE using statistical experimental methods. Process Biochem 40:2757-2762
    • (2005) Process Biochem , vol.40 , pp. 2757-2762
    • Liu, J.G.1    Xing, J.M.2    Chang, T.S.3    Ma, Z.Y.4    Liu, H.Z.5
  • 97
    • 0029047110 scopus 로고
    • Cardiovascular pharmacology (XIII). The efficacy of different thrombolytic drugs in the treatment of acute myocardial infarct
    • 9324694 1:STN:280:DyaK2svmsVWltA%3D%3D
    • Lopez-Sendon J, de Lopez SE, Bobadilla JF, Rubio R, Bermejo J, Delcan JL (1995) Cardiovascular pharmacology (XIII). The efficacy of different thrombolytic drugs in the treatment of acute myocardial infarct. Rev Esp Cardiol 48:407-439
    • (1995) Rev Esp Cardiol , vol.48 , pp. 407-439
    • Lopez-Sendon, J.1    De Lopez, S.E.2    Bobadilla, J.F.3    Rubio, R.4    Bermejo, J.5    Delcan, J.L.6
  • 98
    • 77954798853 scopus 로고    scopus 로고
    • Purification and characterization of a novel fibrinolytic protease from Schizophyllum commune
    • 1:CAS:528:DC%2BC3cXhtVais7vM
    • Lu CL, Chen S, Chen SN (2010a) Purification and characterization of a novel fibrinolytic protease from Schizophyllum commune. J Food Drug Analysis 18:69-76
    • (2010) J Food Drug Analysis , vol.18 , pp. 69-76
    • Lu, C.L.1    Chen, S.2    Chen, S.N.3
  • 99
    • 78149285759 scopus 로고    scopus 로고
    • Purification and characterization of a novel anticoagulant and fibrinolytic enzyme produced by endophytic bacterium Paenibacillus polymyxa EJS-3
    • 10.1016/j.thromres.2010.08.003 1:CAS:528:DC%2BC3cXhtl2gtrnE
    • Lu F, Lu Z, Bie X, Yao Z, Wang Y, Lu Y, Guo Y (2010b) Purification and characterization of a novel anticoagulant and fibrinolytic enzyme produced by endophytic bacterium Paenibacillus polymyxa EJS-3. Thromb Res 126:349-355
    • (2010) Thromb Res , vol.126 , pp. 349-355
    • Lu, F.1    Lu, Z.2    Bie, X.3    Yao, Z.4    Wang, Y.5    Lu, Y.6    Guo, Y.7
  • 100
    • 34248995294 scopus 로고    scopus 로고
    • Isolation and identification of an endophytic strain EJS-3 producing novel fibrinolytic enzymes
    • 17487531 1:CAS:528:DC%2BD2sXlsVGgurY%3D 10.1007/s00284-006-0591-7
    • Lu F, Sun L, Lu Z, Bie X, Fang Y, Liu S (2007) Isolation and identification of an endophytic strain EJS-3 producing novel fibrinolytic enzymes. Curr Microbiol 54:435-439
    • (2007) Curr Microbiol , vol.54 , pp. 435-439
    • Lu, F.1    Sun, L.2    Lu, Z.3    Bie, X.4    Fang, Y.5    Liu, S.6
  • 101
    • 0004330675 scopus 로고
    • Observations on fibrinolysis: Plasminogen, plasmin, and antiplasmin content of human blood
    • 21001709 1:STN:280:DyaH28%2FhvFyitg%3D%3D 10.1016/S0140-6736(46)91017-3
    • Macfarlane RG, Piling J (1946) Observations on fibrinolysis: plasminogen, plasmin, and antiplasmin content of human blood. Lancet 2:562
    • (1946) Lancet , vol.2 , pp. 562
    • Macfarlane, R.G.1    Piling, J.2
  • 103
    • 79959706710 scopus 로고    scopus 로고
    • Production of nattokinase using B. natto NRRL 3666: Media optimization, scale up and kinetic modeling
    • 1:CAS:528:DC%2BC3MXjs1ektg%3D%3D 10.1007/s10068-010-0226-4
    • Mahajan PM, Gokhale SV, Lele SS (2010) Production of nattokinase using B. natto NRRL 3666: media optimization, scale up and kinetic modeling. Food Sci Biotechnol 19:1593-1603
    • (2010) Food Sci Biotechnol , vol.19 , pp. 1593-1603
    • Mahajan, P.M.1    Gokhale, S.V.2    Lele, S.S.3
  • 104
    • 0027584977 scopus 로고
    • Polymorphism of the streptokinase gene-implications for the pathogenesis of poststreptococcal lomerulonephritis
    • 8347929 1:CAS:528:DyaK3sXmtVSks7w%3D 10.1016/S0934-8840(11)80842-X
    • Malke H (1993) Polymorphism of the streptokinase gene-implications for the pathogenesis of poststreptococcal lomerulonephritis. Zentralbl Bakteriol 278:246-257
    • (1993) Zentralbl Bakteriol , vol.278 , pp. 246-257
    • Malke, H.1
  • 105
    • 0021885514 scopus 로고
    • Nucleotide sequence of the streptokinase gene from Streptococcus equisimilis H46A
    • 2989113 1:CAS:528:DyaL2MXkvVams7Y%3D 10.1016/0378-1119(85)90145-3
    • Malke H, Roe B, Ferretti J (1985) Nucleotide sequence of the streptokinase gene from Streptococcus equisimilis H46A. Gene 34:357-362
    • (1985) Gene , vol.34 , pp. 357-362
    • Malke, H.1    Roe, B.2    Ferretti, J.3
  • 106
    • 79957861025 scopus 로고    scopus 로고
    • A low molecular weight chymotrypsin-like novel fibrinolytic enzyme from Streptomyces sp. CS624
    • 1:CAS:528:DC%2BC3MXmvFWltrk%3D 10.1016/j.procbio.2011.03.016
    • Mander P, Cho SS, Simkhada JR, Choi YH, Yoo JC (2011) A low molecular weight chymotrypsin-like novel fibrinolytic enzyme from Streptomyces sp. CS624. Process Biochem 46:1449-1455
    • (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
  • 107
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • 9839663 1:CAS:528:DyaK1cXnsF2ksrw%3D 10.1016/S0041-0101(98)00126-3
    • Markland FS (1998) Snake venoms and the hemostatic system. Toxicon 36:1749-1800
    • (1998) Toxicon , vol.36 , pp. 1749-1800
    • Markland, F.S.1
  • 108
    • 0017692338 scopus 로고
    • The rapid fibrin plate - A method for plasminogen activator assay
    • 1:CAS:528:DyaE1cXitFSh
    • Marsh NA, Gaffney NJ (1977) The rapid fibrin plate - a method for plasminogen activator assay. Thromb Haemostat 38:545-551
    • (1977) Thromb Haemostat , vol.38 , pp. 545-551
    • Marsh, N.A.1    Gaffney, N.J.2
  • 109
    • 0033226386 scopus 로고    scopus 로고
    • A fibrinolytic enzyme from a marine green alga, Codium latum
    • 10643667 1:CAS:528:DC%2BD3cXks1Wquw%3D%3D 10.1016/S0031-9422(99)00356-8
    • Matsubara K, Hori K, Matsuura Y, Miyazawa K (1999) A fibrinolytic enzyme from a marine green alga, Codium latum. Phytochemistry 52(6):993-999
    • (1999) Phytochemistry , vol.52 , Issue.6 , pp. 993-999
    • Matsubara, K.1    Hori, K.2    Matsuura, Y.3    Miyazawa, K.4
  • 110
    • 0034129048 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic enzyme and identification of fibrinogen clotting enzyme in a marine green alga, Codium divaricatum
    • 1:STN:280:DC%2BD3cvotFCgtQ%3D%3D 10.1016/S0305-0491(99)00161-3
    • Matsubara K, Hori K, Matsuura Y, Miyazawa K (2000) Purification and characterization of a fibrinolytic enzyme and identification of fibrinogen clotting enzyme in a marine green alga, Codium divaricatum. Comp Biochem Physiol Biochem Mol Biol 125(1):137-143
    • (2000) Comp Biochem Physiol Biochem Mol Biol , vol.125 , Issue.1 , pp. 137-143
    • Matsubara, K.1    Hori, K.2    Matsuura, Y.3    Miyazawa, K.4
  • 111
    • 0031913551 scopus 로고    scopus 로고
    • Purification and characterization of two fibrinolytic enzymes from a marine green alga, Codium intricatum
    • 10.1016/S0305-0491(97)00303-9
    • Matsubara K, Sumi H, Hori K, Miyazawa K (1998) Purification and characterization of two fibrinolytic enzymes from a marine green alga, Codium intricatum. Comp Biochem Physiol Biochem Mol Biol 119:177-181
    • (1998) Comp Biochem Physiol Biochem Mol Biol , vol.119 , pp. 177-181
    • Matsubara, K.1    Sumi, H.2    Hori, K.3    Miyazawa, K.4
  • 112
    • 0025134741 scopus 로고
    • Evaluation of Serratia peptidase in acute or chronic inflammation of otorhinolaryngology pathology: A multicentre, doubleblind, randomized trial versus placebo
    • 2257960 1:STN:280:DyaK3M%2FnvVGitA%3D%3D
    • Mazzone A, Catalani M, Costanzo M, Drusian A, Mandoli A, Russo S, Guarini E, Vesperini G (1990) Evaluation of Serratia peptidase in acute or chronic inflammation of otorhinolaryngology pathology: a multicentre, doubleblind, randomized trial versus placebo. J Int Med Res 18:379-388
    • (1990) J Int Med Res , vol.18 , pp. 379-388
    • Mazzone, A.1    Catalani, M.2    Costanzo, M.3    Drusian, A.4    Mandoli, A.5    Russo, S.6    Guarini, E.7    Vesperini, G.8
  • 113
    • 0025988405 scopus 로고
    • Streptokinases produced by pathogenic group C streptococci demonstrate species-specific plasminogen activation
    • 1869838 1:CAS:528:DyaK3MXmtVarur8%3D 10.1093/infdis/164.3.515
    • McCoy HE, Broder CC, Lottenberg R (1991) Streptokinases produced by pathogenic group C streptococci demonstrate species-specific plasminogen activation. J Infect Dis 164:515-521
    • (1991) J Infect Dis , vol.164 , pp. 515-521
    • McCoy, H.E.1    Broder, C.C.2    Lottenberg, R.3
  • 115
    • 0020628804 scopus 로고
    • The comparison of solid phase and fibrin plate methods for the measurement of plasminogen activators
    • 6351344 1:CAS:528:DyaL3sXks1Kgt7Y%3D 10.1016/0049-3848(83)90177-9
    • Millar WT, Smith JF (1983) The comparison of solid phase and fibrin plate methods for the measurement of plasminogen activators. Thromb Res 30:431-439
    • (1983) Thromb Res , vol.30 , pp. 431-439
    • Millar, W.T.1    Smith, J.F.2
  • 116
    • 0011908975 scopus 로고
    • Serratia protease. Part I. Purification and general properties of the enzyme
    • 1:CAS:528:DyaE3cXktlWksbg%3D 10.1271/bbb1961.34.310
    • Miyata K, Maejima K, Tomoda K, Isono M (1970) Serratia protease. Part I. Purification and general properties of the enzyme. Agricul Biolog Chemistry 34(2):310-318
    • (1970) Agricul Biolog Chemistry , vol.34 , Issue.2 , pp. 310-318
    • Miyata, K.1    Maejima, K.2    Tomoda, K.3    Isono, M.4
  • 118
    • 0025094123 scopus 로고
    • Duplication of the streptokinase gene in the chromosome of Streptococcus equisimilis H46A
    • 10.1016/0378-1097(90)90348-T
    • Muller J, Malke H (1990) Duplication of the streptokinase gene in the chromosome of Streptococcus equisimilis H46A. FEMS Microbiol Lett 72:75-78
    • (1990) FEMS Microbiol Lett , vol.72 , pp. 75-78
    • Muller, J.1    Malke, H.2
  • 120
    • 0026950259 scopus 로고
    • Nucleotide sequence of the subtilisin NAT gene, aprN, of Bacillus subtilis (natto)
    • 1369081 1:CAS:528:DyaK3sXkvV2qsLc%3D 10.1271/bbb.56.1869
    • Nakamura T, Yamagata Y, Ichishima E (1992) Nucleotide sequence of the subtilisin NAT gene, aprN, of Bacillus subtilis (natto). Biosci Biotechnol Biochem 56(11):1869-1871
    • (1992) Biosci Biotechnol Biochem , vol.56 , Issue.11 , pp. 1869-1871
    • Nakamura, T.1    Yamagata, Y.2    Ichishima, E.3
  • 121
    • 0018099534 scopus 로고
    • Fluorogenic substrates for sensitive and differential estimation of urokinase and tissue plasminogen activator
    • 1:CAS:528:DyaE1cXlt1CqurY%3D
    • Nieuwenhuizen W, Wijngaards G, Groeneverd E (1978) Fluorogenic substrates for sensitive and differential estimation of urokinase and tissue plasminogen activator. Haemost 7:146-149
    • (1978) Haemost , vol.7 , pp. 146-149
    • Nieuwenhuizen, W.1    Wijngaards, G.2    Groeneverd, E.3
  • 122
    • 0031911761 scopus 로고    scopus 로고
    • Role of the amino-terminal region of streptokinase in the generation of a fully functional plasminogen activator complex probed with synthetic peptides
    • 9541396 1:CAS:528:DyaK1cXhvV2lu7g%3D 10.1002/pro.5560070313
    • Nihalani D, Kumar R, Rajagopal K, Sahni G (1998) Role of the amino-terminal region of streptokinase in the generation of a fully functional plasminogen activator complex probed with synthetic peptides. Protein Sci 7:637-648
    • (1998) Protein Sci , vol.7 , pp. 637-648
    • Nihalani, D.1    Kumar, R.2    Rajagopal, K.3    Sahni, G.4
  • 123
    • 0029620638 scopus 로고
    • Streptokinase contains two independent plasminogen-binding sites
    • 8554583 1:CAS:528:DyaK28XhsVWgsw%3D%3D 10.1006/bbrc.1995.2902
    • Nihalani D, Sahni G (1995) Streptokinase contains two independent plasminogen-binding sites. Biochem Biophys Res Commun 217:1245-1254
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 1245-1254
    • Nihalani, D.1    Sahni, G.2
  • 124
    • 0018858619 scopus 로고
    • A sensitive colorimetric assay for various proteases using naphthyl ester derivatives as substrates
    • Ninobe M, Hitomi Y, Fujii S (1980) A sensitive colorimetric assay for various proteases using naphthyl ester derivatives as substrates. J Biochem 87:779-783
    • (1980) J Biochem , vol.87 , pp. 779-783
    • Ninobe, M.1    Hitomi, Y.2    Fujii, S.3
  • 125
    • 0010424856 scopus 로고    scopus 로고
    • Isolation of fibrinolytic enzyme producing strains from kimchi
    • Noh KA, Kim DH, Choi NS, Kim SH (1999) Isolation of fibrinolytic enzyme producing strains from kimchi. Kor J Food Sci Technol 31:219-223
    • (1999) Kor J Food Sci Technol , vol.31 , pp. 219-223
    • Noh, K.A.1    Kim, D.H.2    Choi, N.S.3    Kim, S.H.4
  • 126
    • 0030775983 scopus 로고    scopus 로고
    • Amino acid sequences of metalloendopeptidases specific for acyl-lysine bonds from Grifola frondosa and Pleurotus ostreatus fruiting bodies
    • 1:CAS:528:DyaK2sXnslGht7s%3D 10.1074/jbc.272.48.30032
    • Nonaka T, Dohmae N, Hashimoto Y, Takio K (1997) Amino acid sequences of metalloendopeptidases specific for acyl-lysine bonds from Grifola frondosa and Pleurotus ostreatus fruiting bodies. J Biol chemistry 272:30032-30039
    • (1997) J Biol Chemistry , vol.272 , pp. 30032-30039
    • Nonaka, T.1    Dohmae, N.2    Hashimoto, Y.3    Takio, K.4
  • 127
    • 4444263028 scopus 로고    scopus 로고
    • Purification and characterization of the fibrinolytic enzyme produced by Bacillus subtilis KCK-7 from Chungkookjang
    • 1:CAS:528:DC%2BD2cXot1ygtrg%3D
    • Paik HD, Lee SK, Heo S, Kim SY, Lee H, Kwon TJ (2004) Purification and characterization of the fibrinolytic enzyme produced by Bacillus subtilis KCK-7 from Chungkookjang. J Microbiol Biotechnol 14(4):829-835
    • (2004) J Microbiol Biotechnol , vol.14 , Issue.4 , pp. 829-835
    • Paik, H.D.1    Lee, S.K.2    Heo, S.3    Kim, S.Y.4    Lee, H.5    Kwon, T.J.6
  • 129
    • 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
    • 10.1016/S1096-4959(02)00183-5
    • Peng Y, Huang Q, Zhang RH, Zhang YZ (2003) Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food. Comp Biochem Physiol Biochem Mol Biol 134:45-52
    • (2003) Comp Biochem Physiol Biochem Mol Biol , vol.134 , pp. 45-52
    • Peng, Y.1    Huang, Q.2    Zhang, R.H.3    Zhang, Y.Z.4
  • 130
    • 1842418551 scopus 로고    scopus 로고
    • Cloning and expression of a fibrinolytic enzyme (subtilisin DFE) gene from Bacillus amyloliquefaciens DC-4 in Bacillus subtilis
    • 15059629 1:CAS:528:DC%2BD2cXivVWksL0%3D 10.1016/j.resmic.2003.10.004
    • Peng Y, Yang XJ, Xiao L, Zhang YZ (2004) Cloning and expression of a fibrinolytic enzyme (subtilisin DFE) gene from Bacillus amyloliquefaciens DC-4 in Bacillus subtilis. Res Microbiol 155(3):167-173
    • (2004) Res Microbiol , vol.155 , Issue.3 , pp. 167-173
    • Peng, Y.1    Yang, X.J.2    Xiao, L.3    Zhang, Y.Z.4
  • 131
    • 22644440308 scopus 로고    scopus 로고
    • Cloning and expression in E. coli of coding sequence of the fibrinolytic enzyme mature peptide from Bacillus amyloliquefaciens DC-4
    • 1:CAS:528:DC%2BD3sXkslGrtL8%3D
    • Peng Y, Zhang YZ (2002) Cloning and expression in E. coli of coding sequence of the fibrinolytic enzyme mature peptide from Bacillus amyloliquefaciens DC-4. Chin J Appl Environ Biol 8:285-289
    • (2002) Chin J Appl Environ Biol , vol.8 , pp. 285-289
    • Peng, Y.1    Zhang, Y.Z.2
  • 132
    • 0015810442 scopus 로고
    • Amidase activity of urokinase. I. Hydrolysis of alpha-N-acetyl-l-lysine p-nitroanilide
    • 4762254 1:CAS:528:DyaE3sXlt1aqsrY%3D
    • Petkov D, Christova E, Karadjova M (1973) Amidase activity of urokinase. I. Hydrolysis of alpha-N-acetyl-l-lysine p-nitroanilide. Thromb Diath Haemorrh 29:276-285
    • (1973) Thromb Diath Haemorrh , vol.29 , pp. 276-285
    • Petkov, D.1    Christova, E.2    Karadjova, M.3
  • 133
    • 0034053424 scopus 로고    scopus 로고
    • Characteristics of glycosylated streptokinase secreted from Pichia pastoris: Enhanced resistance of SK to proteolysis by glycosylation
    • 10803905 1:CAS:528:DC%2BD3cXivFWhsrs%3D 10.1007/s002530051643
    • Pratap J, Rajamohan G, Dikshit KL (2000) Characteristics of glycosylated streptokinase secreted from Pichia pastoris: enhanced resistance of SK to proteolysis by glycosylation. Appl Microbiol Biotechnol 53:469-475
    • (2000) Appl Microbiol Biotechnol , vol.53 , pp. 469-475
    • Pratap, J.1    Rajamohan, G.2    Dikshit, K.L.3
  • 134
    • 84880505965 scopus 로고
    • Studies on a proteolytic enzyme in human plasma. VIII. The effect of calcium and strontium ions on the activation of the plasma proteolytic enzyme
    • 1:CAS:528:DyaG38XmslaktA%3D%3D 10.1084/jem.96.4.319
    • Ratnoff OD (1952) Studies on a proteolytic enzyme in human plasma. VIII. The effect of calcium and strontium ions on the activation of the plasma proteolytic enzyme. J Exp Med 96:319
    • (1952) J Exp Med , vol.96 , pp. 319
    • Ratnoff, O.D.1
  • 135
    • 0034609554 scopus 로고    scopus 로고
    • The streptokinase beta domain plays a critical role in activator complex formation and substrate docking
    • 10.1161/01.CIR.102.10.1151
    • Robinson BR, Liu L, Houng AK, Sazanova IY, Reed GL (2000) The streptokinase beta domain plays a critical role in activator complex formation and substrate docking. Circulation 102:490
    • (2000) Circulation , vol.102 , pp. 490
    • Robinson, B.R.1    Liu, L.2    Houng, A.K.3    Sazanova, I.Y.4    Reed, G.L.5
  • 136
    • 0018563587 scopus 로고
    • Protein analysis of earthworm coelomic fluid: I. Polymorphic system of the natural hemolysin of Eisenia fetida andrei
    • 1:CAS:528:DyaL3cXhsVeksr0%3D 10.1016/S0145-305X(79)80055-5
    • Roch P (1979) Protein analysis of earthworm coelomic fluid: I. Polymorphic system of the natural hemolysin of Eisenia fetida andrei. Devel Comp Immun 3:599-608
    • (1979) Devel Comp Immun , vol.3 , pp. 599-608
    • Roch, P.1
  • 137
    • 0020605972 scopus 로고
    • A rapid and highly sensitive solid-phase radioassay for plasminogen activators
    • 6685354 1:CAS:528:DyaL3sXlvFSgsro%3D 10.1016/0049-3848(83)90329-8
    • Roche PL, Compeau JD, Schaw ST (1983) A rapid and highly sensitive solid-phase radioassay for plasminogen activators. Thromb Res 31:269-277
    • (1983) Thromb Res , vol.31 , pp. 269-277
    • Roche, P.L.1    Compeau, J.D.2    Schaw, S.T.3
  • 138
    • 0028213355 scopus 로고
    • Characterization of fibrinolytic activities of Treponema denticola
    • 8168936 1:CAS:528:DyaK2cXktVClt7o%3D
    • Rosen G, Naor R, Kutner S, Sela MN (1994) Characterization of fibrinolytic activities of Treponema denticola. Infect Immun 62(5):1749-1754
    • (1994) Infect Immun , vol.62 , Issue.5 , pp. 1749-1754
    • Rosen, G.1    Naor, R.2    Kutner, S.3    Sela, M.N.4
  • 139
    • 11844278415 scopus 로고    scopus 로고
    • Production of fibrinolytic enzyme from soybean grits fermented by Bacillus firmus NA-1
    • 15671687 1:CAS:528:DC%2BD2MXhtVOnu7c%3D 10.1089/jmf.2004.7.442
    • Seo JH, Lee SP (2004) Production of fibrinolytic enzyme from soybean grits fermented by Bacillus firmus NA-1. J Med Food 7(4):442-449
    • (2004) J Med Food , vol.7 , Issue.4 , pp. 442-449
    • Seo, J.H.1    Lee, S.P.2
  • 140
    • 0014033251 scopus 로고
    • Activity of plasmin and streptokinase-activator on substituted arginine and lysine esters
    • 1:CAS:528:DyaF28XksFyitLY%3D
    • Sherry S, Alkjaersig N, Fletcher AP (1966) Activity of plasmin and streptokinase-activator on substituted arginine and lysine esters. Throm Diath Haemorrh 16:18-31
    • (1966) Throm Diath Haemorrh , vol.16 , pp. 18-31
    • Sherry, S.1    Alkjaersig, N.2    Fletcher, A.P.3
  • 141
    • 0001595590 scopus 로고
    • Studies on enhanced fibrinolytic activity in man
    • 13654517 1:CAS:528:DyaG1MXhtVWjsbg%3D 10.1172/JCI103863
    • Sherry S, Lindemeyer RI, Fletcher AP, Alkjaersig N (1959) Studies on enhanced fibrinolytic activity in man. J Clin Invest 38:810
    • (1959) J Clin Invest , vol.38 , pp. 810
    • Sherry, S.1    Lindemeyer, R.I.2    Fletcher, A.P.3    Alkjaersig, N.4
  • 142
    • 0027985626 scopus 로고
    • Function of streptokinase fragments in plasminogen activation
    • 7998939 1:CAS:528:DyaK2cXmslOgurY%3D
    • Shi GY, Chang BI, Chen SM, Wu DH, Wu HL (1994) Function of streptokinase fragments in plasminogen activation. Biochem J 304:235-241
    • (1994) Biochem J , vol.304 , pp. 235-241
    • Shi, G.Y.1    Chang, B.I.2    Chen, S.M.3    Wu, D.H.4    Wu, H.L.5
  • 143
    • 70450221689 scopus 로고    scopus 로고
    • A novel fibrinolytic protease from Streptomyces sp. CS684
    • 1:CAS:528:DC%2BD1MXhsVGrurzE 10.1016/j.procbio.2009.08.010
    • Simkhada JR, Mander P, Cho SS, Yoo JC (2010) A novel fibrinolytic protease from Streptomyces sp. CS684. Process Biochem 45:88-93
    • (2010) Process Biochem , vol.45 , pp. 88-93
    • Simkhada, J.R.1    Mander, P.2    Cho, S.S.3    Yoo, J.C.4
  • 144
    • 0019864396 scopus 로고
    • Fibrinolysis with acyl-enzymes - A new approach to thrombolytic therapy
    • 7219537 1:CAS:528:DyaL3MXkvFSqsLc%3D 10.1038/290505a0
    • Smith RAG, Dupe RJ, English PD, Green J (1981) Fibrinolysis with acyl-enzymes - a new approach to thrombolytic therapy. Nature 290:505-508
    • (1981) Nature , vol.290 , pp. 505-508
    • Smith, R.A.G.1    Dupe, R.J.2    English, P.D.3    Green, J.4
  • 145
    • 0015386158 scopus 로고
    • A technique for demonstrating fibrinolysis by cutaneous bacteria
    • 5076811 1:CAS:528:DyaE3sXhtlGhsg%3D%3D 10.1136/jcp.25.8.740
    • Somerville DA (1972) A technique for demonstrating fibrinolysis by cutaneous bacteria. J Clin Pathol 25:740-741
    • (1972) J Clin Pathol , vol.25 , pp. 740-741
    • Somerville, D.A.1
  • 146
    • 0025134853 scopus 로고
    • Enhancement of the fibrinolytic activity in plasma by oral administration of nattokinase
    • 2123064 1:CAS:528:DyaK3MXit1Squ7k%3D 10.1159/000205051
    • Sumi H, Hamada H, Nakanishi K, Hiratani H (1990) Enhancement of the fibrinolytic activity in plasma by oral administration of nattokinase. Acta Haematol 84(3):139-143
    • (1990) Acta Haematol , vol.84 , Issue.3 , pp. 139-143
    • Sumi, H.1    Hamada, H.2    Nakanishi, K.3    Hiratani, H.4
  • 147
    • 0023656415 scopus 로고
    • A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto; A typical and popular soybean food in the Japanese diet
    • 3478223 1:CAS:528:DyaL1cXitVemsrw%3D 10.1007/BF01956052
    • Sumi H, Hamada H, Tsushima H, Mihara H, Muraki H (1987) A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto; a typical and popular soybean food in the Japanese diet. Experientia 43(10):1110-1111
    • (1987) Experientia , vol.43 , Issue.10 , pp. 1110-1111
    • Sumi, H.1    Hamada, H.2    Tsushima, H.3    Mihara, H.4    Muraki, H.5
  • 148
    • 15744374608 scopus 로고
    • In vitro and in vivo fibrinolytic properties of nattokinase
    • Sumi H, Nakajima N, Mihara H (1992) In vitro and in vivo fibrinolytic properties of nattokinase. Thromb Haemost 89:1267
    • (1992) Thromb Haemost , vol.89 , pp. 1267
    • Sumi, H.1    Nakajima, N.2    Mihara, H.3
  • 149
    • 0042232551 scopus 로고    scopus 로고
    • Domain truncation studies reveal that the streptokinase-plasmin activator complex utilizes long range protein-protein interactions with macromolecular substrate to maximize catalytic turnover
    • 12773528 1:CAS:528:DC%2BD3sXmtFeqsrg%3D 10.1074/jbc.M303799200
    • Sundram V, Nanda JS, Rajagopal K, Dhar J, Chaudhary A, Sahni G (2003) Domain truncation studies reveal that the streptokinase-plasmin activator complex utilizes long range protein-protein interactions with macromolecular substrate to maximize catalytic turnover. J Biol Chem 278:30569-30577
    • (2003) J Biol Chem , vol.278 , pp. 30569-30577
    • Sundram, V.1    Nanda, J.S.2    Rajagopal, K.3    Dhar, J.4    Chaudhary, A.5    Sahni, G.6
  • 150
    • 0037373954 scopus 로고    scopus 로고
    • Dietary supplementation with fermented soybeans suppresses intimal thickening
    • 12620531 1:CAS:528:DC%2BD3sXhsVanurY%3D 10.1016/S0899-9007(02)00853-5
    • Suzuki Y, Kondo K, Ichise H, Tsukamoto Y, Urano T, Umemura K (2003) Dietary supplementation with fermented soybeans suppresses intimal thickening. Nutrition 19:261-264
    • (2003) Nutrition , vol.19 , pp. 261-264
    • Suzuki, Y.1    Kondo, K.2    Ichise, H.3    Tsukamoto, Y.4    Urano, T.5    Umemura, K.6
  • 151
    • 0030906693 scopus 로고    scopus 로고
    • Solid state fermentation of rice chaff for fibrinolytic enzyme production by Fusarium oxysporum
    • 1:CAS:528:DyaK2sXjslGns7s%3D 10.1023/A:1018352328874
    • Tao S, Peng L, Beihui L, Deming L, Zuohu L (1997) Solid state fermentation of rice chaff for fibrinolytic enzyme production by Fusarium oxysporum. Biotechnol Lett 19(5):465-467
    • (1997) Biotechnol Lett , vol.19 , Issue.5 , pp. 465-467
    • Tao, S.1    Peng, L.2    Beihui, L.3    Deming, L.4    Zuohu, L.5
  • 152
    • 2442473557 scopus 로고    scopus 로고
    • Successive cultivation of Fusarium oxysporum on rice chaff for economic production of fibrinolytic enzyme
    • 1:CAS:528:DyaK1cXislWmt7k%3D
    • Tao S, Peng L, Beihui L, Deming L, Zuohu L (1998) Successive cultivation of Fusarium oxysporum on rice chaff for economic production of fibrinolytic enzyme. Bioprocess Eng 18(5):379-381
    • (1998) Bioprocess Eng , vol.18 , Issue.5 , pp. 379-381
    • Tao, S.1    Peng, L.2    Beihui, L.3    Deming, L.4    Zuohu, L.5
  • 153
    • 34848879197 scopus 로고    scopus 로고
    • Purification and biochemical characterization of fibrinolytic enzyme produced by thermophilic fungus Oidiodendron flavum
    • 1:CAS:528:DC%2BD28XlvVyitLY%3D 10.3923/biotech.2006.160.165
    • Tharwat NA (2006) Purification and biochemical characterization of fibrinolytic enzyme produced by thermophilic fungus Oidiodendron flavum. Biotechnol 5(2):160-165
    • (2006) Biotechnol , vol.5 , Issue.2 , pp. 160-165
    • Tharwat, N.A.1
  • 154
    • 33846799494 scopus 로고    scopus 로고
    • Purification and characterization of fibrinolytic alkaline protease from Fusarium sp. BLB
    • 17221202 1:CAS:528:DC%2BD2sXht1yhu78%3D 10.1007/s00253-006-0621-1
    • Ueda M, Kubo T, Miyatake K, Nakamura T (2007) Purification and characterization of fibrinolytic alkaline protease from Fusarium sp. BLB. Appl Microbiol Biotechnol 74:331-338
    • (2007) Appl Microbiol Biotechnol , vol.74 , pp. 331-338
    • Ueda, M.1    Kubo, T.2    Miyatake, K.3    Nakamura, T.4
  • 155
    • 78149408229 scopus 로고    scopus 로고
    • Highly potent fibrinolytic serine protease from Streptomyces
    • 22112764 1:CAS:528:DC%2BC3cXhtl2isL3N 10.1016/j.enzmictec.2010.08.003
    • Uesugi Y, Usuki H, Iwabuchi M, Hatanaka T (2011) Highly potent fibrinolytic serine protease from Streptomyces. Enzyme Microb Technol 48:7-12
    • (2011) Enzyme Microb Technol , vol.48 , pp. 7-12
    • Uesugi, Y.1    Usuki, H.2    Iwabuchi, M.3    Hatanaka, T.4
  • 156
    • 0036762862 scopus 로고    scopus 로고
    • Effects of deletion of streptokinase residues 48-59 on plasminogen activation
    • 12456874 1:CAS:528:DC%2BD38XptlOhtbw%3D 10.1093/protein/15.9.753
    • Wakeham N, Terzyan S, Zhai PZ, Loy JA, Tang J, Zhang XC (2002) Effects of deletion of streptokinase residues 48-59 on plasminogen activation. Protein Eng 15:753-761
    • (2002) Protein Eng , vol.15 , pp. 753-761
    • Wakeham, N.1    Terzyan, S.2    Zhai, P.Z.3    Loy, J.A.4    Tang, J.5    Zhang, X.C.6
  • 158
    • 33746315610 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic enzyme of Bacillus subtilis DC33, isolated from Chinese traditional douchi
    • 16575557 1:CAS:528:DC%2BD28Xnt1aisLg%3D 10.1007/s10295-006-0111-6
    • Wang CT, Ji BP, Li B, Nout R, Li PL, Ji H, Chen LF (2006) Purification and characterization of a fibrinolytic enzyme of Bacillus subtilis DC33, isolated from Chinese traditional douchi. J Ind Microbiol Biotechnol 33:750-758
    • (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
  • 159
    • 0033256485 scopus 로고    scopus 로고
    • Purification and characterization of a novel fibrinolytic enzyme from Streptomyces spp
    • 10719627 1:CAS:528:DyaK1MXitFWmsbo%3D
    • Wang J, Wang M, Wang Y (1999a) Purification and characterization of a novel fibrinolytic enzyme from Streptomyces spp. Chin J Biotechnol 15(2):83-89
    • (1999) Chin J Biotechnol , vol.15 , Issue.2 , pp. 83-89
    • Wang, J.1    Wang, M.2    Wang, Y.3
  • 160
    • 0024433888 scopus 로고
    • Hematological studies on naturally occurring substances II. Eject of animal crude drugs on blood coagulation and fibrinolysis systems
    • 2598329 1:STN:280:DyaK3c%2FptVOlsg%3D%3D 10.1248/cpb.37.2236
    • Wang JD, Narui T, Kurata H, Taeuchi K, Hashimoto T, Okuyama T (1989) Hematological studies on naturally occurring substances II. Eject of animal crude drugs on blood coagulation and fibrinolysis systems. Chem Pharm Bull 37:2236-2238
    • (1989) Chem Pharm Bull , vol.37 , pp. 2236-2238
    • Wang, J.D.1    Narui, T.2    Kurata, H.3    Taeuchi, K.4    Hashimoto, T.5    Okuyama, T.6
  • 161
    • 58049204410 scopus 로고    scopus 로고
    • A novel nattokinase produced by Pseudomonas sp. TKU015 using shrimp shells as substrate
    • 1:CAS:528:DC%2BD1MXht1Cqug%3D%3D 10.1016/j.procbio.2008.09.009
    • Wang S, Chen H, Liang T, Lin Y (2009) A novel nattokinase produced by Pseudomonas sp. TKU015 using shrimp shells as substrate. Process Biochem 44:70-76
    • (2009) Process Biochem , vol.44 , pp. 70-76
    • Wang, S.1    Chen, H.2    Liang, T.3    Lin, Y.4
  • 162
    • 0033586797 scopus 로고    scopus 로고
    • Deletion of Ile1 changes the mechanism of streptokinase: Evidence for the molecular sexuality hypothesis
    • 10213631 1:CAS:528:DyaK1MXitFShtbc%3D 10.1021/bi981915h
    • Wang SG, Reed GL, Hedstrom L (1999b) Deletion of Ile1 changes the mechanism of streptokinase: evidence for the molecular sexuality hypothesis. Biochemistry 38:5232-5240
    • (1999) Biochemistry , vol.38 , pp. 5232-5240
    • Wang, S.G.1    Reed, G.L.2    Hedstrom, L.3
  • 163
    • 41049097333 scopus 로고    scopus 로고
    • Screening of a high fibrinolytic enzyme producing strain and characterization of the fibrinolytic enzyme produced from Bacillus subtilis LD-8547
    • 1:CAS:528:DC%2BD1cXjsFWlt74%3D 10.1007/s11274-007-9496-2
    • Wang SH, Zhang C, Yang YL, Diao M, Bai MF (2008a) Screening of a high fibrinolytic enzyme producing strain and characterization of the fibrinolytic enzyme produced from Bacillus subtilis LD-8547. World J Microbiol Biotechnol 24:475-482
    • (2008) World J Microbiol Biotechnol , vol.24 , pp. 475-482
    • Wang, S.H.1    Zhang, C.2    Yang, Y.L.3    Diao, M.4    Bai, M.F.5
  • 164
    • 43849106650 scopus 로고    scopus 로고
    • Optimization of conditions for protease production by Chryseobacterium taeanense TKU001
    • 1:CAS:528:DC%2BD1cXitlyqtLg%3D 10.1016/j.biortech.2007.07.036
    • Wang SL, Yang CH, Liang TW, Yen YH (2008b) Optimization of conditions for protease production by Chryseobacterium taeanense TKU001. Bioresource Technol 99:3700-3707
    • (2008) Bioresource Technol , vol.99 , pp. 3700-3707
    • Wang, S.L.1    Yang, C.H.2    Liang, T.W.3    Yen, Y.H.4
  • 165
    • 0032508547 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human plasmin complexed with streptokinase
    • 9733510 1:CAS:528:DyaK1cXmtVKitr0%3D 10.1126/science.281.5383.1662
    • Wang X, Lin X, Loy JA, Tang J, Zhang XC (1998) Crystal structure of the catalytic domain of human plasmin complexed with streptokinase. Science 281:1662-1665
    • (1998) Science , vol.281 , pp. 1662-1665
    • Wang, X.1    Lin, X.2    Loy, J.A.3    Tang, J.4    Zhang, X.C.5
  • 166
    • 0028842609 scopus 로고
    • Advances in the use of Bacillus subtilis for the expression and secretion of heterologous proteins
    • 7579663 1:CAS:528:DyaK2MXovVarsbg%3D 10.1016/0958-1669(95)80085-9
    • Wong SL (1995) Advances in the use of Bacillus subtilis for the expression and secretion of heterologous proteins. Curr Opin Biotechnol 6:517-522
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 517-522
    • Wong, S.L.1
  • 167
    • 0021344451 scopus 로고
    • The subtilisin e gene of Bacillus subtilis is transcribed from a sigma-37 promoter in vivo
    • 6322190 1:CAS:528:DyaL2cXitVCgtLY%3D 10.1073/pnas.81.4.1184
    • Wong SL, Price CW, Goldfarb DS, Doi RH (1984) The subtilisin E gene of Bacillus subtilis is transcribed from a sigma-37 promoter in vivo. Proc Natl Acad Sci USA 81:1184-1188
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 1184-1188
    • Wong, S.L.1    Price, C.W.2    Goldfarb, D.S.3    Doi, R.H.4
  • 168
    • 0003457873 scopus 로고    scopus 로고
    • World Health Organization WHO Geneva
    • World Health Organization (2001) The World Health report 2001. WHO, Geneva
    • (2001) The World Health Report 2001
  • 169
    • 61349192174 scopus 로고    scopus 로고
    • Purification and characterization of a novel fibrinolytic protease from Fusarium sp. CPCC 480097
    • 19142678 10.1007/s10295-008-0516-5 1:CAS:528:DC%2BD1MXitlWrs74%3D
    • Wu B, Wu L, Chen D, Yang Z, Luo M (2009) Purification and characterization of a novel fibrinolytic protease from Fusarium sp. CPCC 480097. J Ind Microbiol Biotechnol 36(3):451-459
    • (2009) J Ind Microbiol Biotechnol , vol.36 , Issue.3 , pp. 451-459
    • Wu, B.1    Wu, L.2    Chen, D.3    Yang, Z.4    Luo, M.5
  • 170
    • 0035805508 scopus 로고    scopus 로고
    • Coiled coil region of streptokinase gamma-domain is essential for plasminogen activation
    • 11278293 1:CAS:528:DC%2BD3MXjs1OrsLw%3D 10.1074/jbc.M005935200
    • Wu DH, Shi GY, Chuang WJ, Hsu JM, Young KC, Chang CW, Wu HL (2001) Coiled coil region of streptokinase gamma-domain is essential for plasminogen activation. J Biol Chem 276:15025-15033
    • (2001) J Biol Chem , vol.276 , pp. 15025-15033
    • Wu, D.H.1    Shi, G.Y.2    Chuang, W.J.3    Hsu, J.M.4    Young, K.C.5    Chang, C.W.6    Wu, H.L.7
  • 171
    • 0031951905 scopus 로고    scopus 로고
    • Engineering of plasmin-resistant forms of streptokinase and their production in Bacillus subtilis: Streptokinase with longer functional half-life
    • 9501422 1:CAS:528:DyaK1cXhs1arsb8%3D
    • Wu XC, Ye RQ, Duan YJ, Wong S-L (1998) Engineering of plasmin-resistant forms of streptokinase and their production in Bacillus subtilis: streptokinase with longer functional half-life. Appl Environ Microbiol 64:824-829
    • (1998) Appl Environ Microbiol , vol.64 , pp. 824-829
    • Wu, X.C.1    Ye, R.Q.2    Duan, Y.J.3    Wong, S.-L.4
  • 172
    • 21644432806 scopus 로고    scopus 로고
    • Highly efficient gene expression of a fibrinolytic enzyme (subtilisin DFE) in Bacillus subtilis mediated by the promoter of α-amylase gene from Bacillus amyloliquefaciens
    • 15604765 1:CAS:528:DC%2BD2cXhtVaru7fF 10.1023/B:BILE.0000045634.46909.2b
    • Xiao L, Zhang RH, Peng Y, Zhang YZ (2004) Highly efficient gene expression of a fibrinolytic enzyme (subtilisin DFE) in Bacillus subtilis mediated by the promoter of α-amylase gene from Bacillus amyloliquefaciens. Biotechnol Lett 26:1365-1369
    • (2004) Biotechnol Lett , vol.26 , pp. 1365-1369
    • Xiao, L.1    Zhang, R.H.2    Peng, Y.3    Zhang, Y.Z.4
  • 173
    • 17844395238 scopus 로고    scopus 로고
    • Purification and characterization of a novel fibrinolytic enzyme from Rhizopus chinensis 12
    • 15614557 10.1007/s00253-004-1846-5 1:CAS:528:DC%2BD2MXjtlart7w%3D
    • Xiao-Lan L, Lian-Xiang D, Fu-Ping L, Xi-Qun Z, Jing X (2005) Purification and characterization of a novel fibrinolytic enzyme from Rhizopus chinensis 12. Appl Microbiol Biotechnol 67(2):209-214
    • (2005) Appl Microbiol Biotechnol , vol.67 , Issue.2 , pp. 209-214
    • Xiao-Lan, L.1    Lian-Xiang, D.2    Fu-Ping, L.3    Xi-Qun, Z.4    Jing, X.5
  • 174
    • 0035723632 scopus 로고    scopus 로고
    • Continuous culture studies on the stability and expression of recombinant streptokinase in Escherichia coli
    • 1:CAS:528:DC%2BD38XivFWmtL8%3D 10.1007/s004490100221
    • Yazdani SS, Mukherjee KJ (2002) Continuous culture studies on the stability and expression of recombinant streptokinase in Escherichia coli. Bioprocess Biosyst Eng 24:341-346
    • (2002) Bioprocess Biosyst Eng , vol.24 , pp. 341-346
    • Yazdani, S.S.1    Mukherjee, K.J.2
  • 175
    • 81855185465 scopus 로고    scopus 로고
    • Directed evolution improves the fibrinolytic activity of nattokinase from Bacillus natto
    • 22029857 10.1111/j.1574-6968.2011.02423.x 1:CAS:528:DC%2BC3MXhs1antrvI
    • Yongjun C, Wei B, Shujun J, Meizhi W, Yan J, Yan Y, Zhongliang Z, Goulin Z (2011) Directed evolution improves the fibrinolytic activity of nattokinase from Bacillus natto. FEMS Microbiol Lett 325(2):155-161
    • (2011) FEMS Microbiol Lett , vol.325 , Issue.2 , pp. 155-161
    • Yongjun, C.1    Wei, B.2    Shujun, J.3    Meizhi, W.4    Yan, J.5    Yan, Y.6    Zhongliang, Z.7    Goulin, Z.8
  • 177
    • 0028858105 scopus 로고
    • Interaction of streptokinase and plasminogen-studied with truncated streptokinase peptides
    • 7494004 1:CAS:528:DyaK2MXpvVOgt74%3D 10.1074/jbc.270.49.29601
    • Young KC, Shi GY, Chang YF, Chang BI, Chang LC, Lai MD, Chuang WJ, Wu HL (1995) Interaction of streptokinase and plasminogen-studied with truncated streptokinase peptides. J Biol Chem 270:29601-29606
    • (1995) J Biol Chem , vol.270 , pp. 29601-29606
    • Young, K.C.1    Shi, G.Y.2    Chang, Y.F.3    Chang, B.I.4    Chang, L.C.5    Lai, M.D.6    Chuang, W.J.7    Wu, H.L.8
  • 178
    • 0037435626 scopus 로고    scopus 로고
    • Functional roles of streptokinase C-terminal flexible peptide in active site formation and substrate recognition in plasminogen activation
    • 12515545 1:CAS:528:DC%2BD38XptlWrtbY%3D 10.1021/bi026746m
    • Zhai P, Wakeham N, Loy JA, Zhang XC (2003) Functional roles of streptokinase C-terminal flexible peptide in active site formation and substrate recognition in plasminogen activation. Biochemistry 42:114-120
    • (2003) Biochemistry , vol.42 , pp. 114-120
    • Zhai, P.1    Wakeham, N.2    Loy, J.A.3    Zhang, X.C.4
  • 179
    • 22644447981 scopus 로고    scopus 로고
    • Expression and characteristics of a novel fibrinolytic enzyme (subtilisin DFE) in Escherichia coli
    • 16033520 1:CAS:528:DC%2BD28XhvFGhu7s%3D 10.1111/j.1472-765X.2005.01715.x
    • Zhang RH, Xiao L, Peng Y, Wang HY, Bai F, Zhang YZ (2005) Expression and characteristics of a novel fibrinolytic enzyme (subtilisin DFE) in Escherichia coli. Lett Appl Microbiol 41:190-195
    • (2005) Lett Appl Microbiol , vol.41 , pp. 190-195
    • Zhang, R.H.1    Xiao, L.2    Peng, Y.3    Wang, H.Y.4    Bai, F.5    Zhang, Y.Z.6
  • 180
    • 12844277399 scopus 로고    scopus 로고
    • Construction of a 3D model of nattokinase, a novel fibrinolytic enzyme from Bacillus natto A novel nucleophilic catalytic mechanism for nattokinase
    • 1:CAS:528:DC%2BD2MXmtlGlsg%3D%3D 10.1016/j.jmgm.2004.10.002
    • Zheng ZL, Zuo ZY, Liu ZG, Tsai KC, Liu AF, Zou GL (2005) Construction of a 3D model of nattokinase, a novel fibrinolytic enzyme from Bacillus natto A novel nucleophilic catalytic mechanism for nattokinase. J Mol Graphics 23:373-380
    • (2005) J Mol Graphics , vol.23 , pp. 373-380
    • Zheng, Z.L.1    Zuo, Z.Y.2    Liu, Z.G.3    Tsai, K.C.4    Liu, A.F.5    Zou, G.L.6
  • 181
    • 0024409494 scopus 로고
    • Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process
    • 2657436 1:CAS:528:DyaL1MXksFehsr0%3D 10.1038/339483a0
    • Zhu X, Ohta Y, Jordan F, Inouye M (1989) Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process. Nature 339:483-484
    • (1989) Nature , vol.339 , pp. 483-484
    • Zhu, X.1    Ohta, Y.2    Jordan, F.3    Inouye, M.4
  • 182
    • 0017873119 scopus 로고
    • Direct fluorescent assay of urokinase and plasminogen activators of normal and malignant cells: Kinetics and inhibitor profiles
    • 1:CAS:528:DyaE1cXhsVOqsr8%3D 10.1073/pnas.75.2.750
    • Zimmerman M, Quigley JP, Ashe B, Dron C, Goldfarb R, Troll W (1978) Direct fluorescent assay of urokinase and plasminogen activators of normal and malignant cells: kinetics and inhibitor profiles. Proc Nalt Acad Sci 75:750-753
    • (1978) Proc Nalt Acad Sci , vol.75 , pp. 750-753
    • Zimmerman, M.1    Quigley, J.P.2    Ashe, B.3    Dron, C.4    Goldfarb, R.5    Troll, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.