Evgenia G. Monolithic peptidyl sorbents for comparison of affinity properties of plasminogen activators. Journal of Chromatography B , 1 , Journal of Biological Chemistry , 35 , Anirban Banerjee, Yusuf Chisti, U. C Banerjee. Streptokinase—a clinically useful thrombolytic agent. Biotechnology Advances , 22 4 , Guinn, J. Johnson, V. Ionic modulation of the effects of heparin and 6-aminohexanoic acid on plasminogen activation by streptokinase: The role of ionic strength, divalent cations and chloride. European Journal of Drug Metabolism and Pharmacokinetics , 28 2 , Structural correlates of a functional streptokinase antigenic epitope: serine is an essential residue for antibody binding.
Journal of Immunological Methods , , Francis J. Castellino, Victoria A. Human Plasminogen: Structure, Activation, and Function.
Table of contents
William F. Thrombolytic Therapy. Verhamme, William P. Fay, Paul E. Journal of Biological Chemistry , 28 , Journal of Biological Chemistry , 18 , Castellino, V. Plasminogen and Streptokinase. Hiremagalur N. Jayaram, Gurpreet S. Ahluwalia, David A. Enzyme Applications, Therapeutic. Boxrud, William P. Journal of Biological Chemistry , 19 , Rutter, B. Carpenter, S. Hill, I. Varidase: the science behind the medicament. Journal of Wound Care , 9 5 , Collen, H. Recent developments in thrombolytic therapy. Fibrinolysis and Proteolysis , 14 , Human plasminogen catalytic domain undergoes an unusual conformational change upon activation.
Journal of Molecular Biology , 4 , Recombinant streptokinase production by fed-batch cultivation of Escherichia coli. Enzyme and Microbial Technology , 24 10 , Plasminogen Activation by Streptokinase via a Unique Mechanism. Journal of Biological Chemistry , 5 , Adam E. Schussheim, Valentin Fuster. Thrombosis, antithrombotic agents, and the antithrombotic approach in cardiac disease. Progress in Cardiovascular Diseases , 40 3 , Leonid V. Medved, Dmitry A.
Solovjov, Kenneth C. Domain Structure, Stability and Interactions in Streptokinase. European Journal of Biochemistry , 2 , Smith, Julian M. Marshall, Christopher P. Ponting, Christopher M. The domain organization of streptokinase: Nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragments.
Protein Science , 5 4 , Paul E.
Bock, Duane E. Day, Ingrid M. Verhamme, M. Margarida Bernardo, Steven T. Olson, Joseph D. Journal of Biological Chemistry , 2 , Pirie-Shepherd, R. Serrano, N. Andon, M. Gonzalez-Gronow, S. The role of carbohydrate in the activation of plasminogen 2 glycoforms by streptokinase. Fibrinolysis , 10 1 , Interaction of Streptokinase and Plasminogen.
Journal of Biological Chemistry , 49 , Sergio Lizano, Kenneth H. Streptokinase-mediated plasminogen activation using a recombinant dual fusion protein construct. A novel approach to study bacterial-host protein interactions. Journal of Microbiological Methods , 23 3 , Jieyi Wang, E.
Structure and function of microplasminogen: II. Determinants of activation by urokinase and by the bacterial activator streptokinase. Protein Science , 4 9 , White, Guy L. Mapping the antigenic regions of streptokinase in humans before and after streptokinase therapy. Molecular Immunology , 32 10 , Plasminogen, absorbed by Escherichia coli expressing curli or by Salmonella enteritidis expressing thin aggregative fimbriae, can be activated by simultaneously captured tissue-type plasminogen activator t-PA. Molecular Microbiology , 14 3 , Streptokinase activates plasminogen bound to human group C and G streptococci through M-like proteins.
The major peak contained fibrinolytic activity Fig. These active fractions were combined and dialyzed against 50 mM sodium phosphate buffer pH 7. This chromatography fractions showed a peak and possessed fibrinolytic activity Fig. The specific activity of the purified enzyme was U mg -1 protein with 8. This yield was higher than the reported fibrinolytic enzyme from Fusarium sp.
The purification procedure of fibrinolytic enzyme was summarized in Table 1. Also, the fibrin zymography showed enzyme activity Fig. The molecular weight of Pseudoalteromonas fibrinolytic enzyme was not previously reported. The molecular weight of reported protease from Pseudoalteromonas sp. The alkaline serine protease derived from the metagenome of Shewanella sp.
Effect of temperature and pH: The fibrinolytic enzyme from the marine isolate, Pseudoalteromonas sp. Also Chang et al. The fibrinolytic enzyme from Pseudoalteromonas sp. Fibrinolytic enzyme activity of Pseudoalteromonas sp. This pH optimum was similar to that of fibrinolytic enzyme from Streptomyces sp. The optimum pH of the isolated fibrinolytic enzymes was higher than that of some of the microbial fibrinolytic enzyme from Bacillus sp.
Previous study demonstrated that the amino acid composition of fibrinolytic enzyme plays an important role in its optimal reaction pH value Wong and Mine, Therefore, it is speculated that in the present study, the Pseudoalteromonas sp. Effect of ions on enzyme activity: In Pseudoalteromonas sp. In Pseudoalteromonas sp. This property was different from the fibrinolytic enzyme of Pseudomonas sp. Plasminogen activator and direct plasmin like activity of fibrinolytic enzyme: The fibrinolytic enzyme from Pseudoalteromonas sp.
The larger zone observed shows that the purified enzyme was able to convert plasminogen to plasmin. According to the present study, the transparent clear zone of plasminogen-rich plate was larger in size than that of plasminogen-free plate Fig. This suggests that, the fibrinolytic enzyme have plasminogen-activator activity and also plasmin like activity. Similar result was also reported with other bacterial species previously Jeong et al.
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In vitro blood clot lytic activity of fibrinolytic enzyme: The blood clot lytic effect of fibrinolytic enzyme was studied in in vitro condition. Clot lysis was not observed in the control vial. The fibrinolytic enzyme digested blood clot effectively at higher doses Fig. The fibrinolytic enzyme activity of B. A potent fibrinolytic enzyme was isolated from Pseudoalteromonas sp. The purified enzyme was active at higher pH ranges and temperature. It digested fibrin net of human blood clot in vitro. This study explores new sources of fibrinolytic enzyme to treat and prevent CVDs.
The author P. Agrebi, R. Haddar, N. Hmidet, K. Jellouli, L. Manni and M. Nasri, BSF1 fibrinolytic enzyme from a marine bacterium Bacillus subtilis A Purification, biochemical and molecular characterization. Process Biochem. Hahn, K. Ryu, J. Kim, I. Kim and Y. Kim, Purification and characterization of a serine protease with fibrinolytic activity from the dung beetles, Catharsius molossus. Thrombosis Res. Mullertz, The fibrin plate method for estimating fibrinolytic activity. Yarzabal, C. Jurgensen, M.http://phon-er.com/js/smartphone-nghe/download-igo-free-for-iphone.php
Fibrinolytic Bacterial Enzymes with Thrombolytic Activity : Essam Kotb :
Bastidas, J. Cruz and J. Puig, Cloning, expression and purification of recombinant streptokinase: Partial characterization of the protein expressed in Escherichia coli Braz. Hoane and P. Dunnill, The formation of protein precipitates and their centrifugal recovery. Chang, C. Fan, F. Kuo and H. Sung, Food Chem. Dey, Potent fibrinolytic enzyme from a thermophilic Streptomyces megasporus strain SD5. Applied Microbiol. Lijnen, Basic and clinical aspects of fibrinolysis and thrombolysis. Blood, Tissue-type plasminogen activator: A historical perspective and personal account.
Thrombosis Haemostasis, 2: 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. Pan, G. Chen, S. Huang, Z. Zhang, Y. Li and Z.
Liang, Biochemical characteristics of a fibrinolytic enzyme purified from a marine bacterium, Bacillus subtilis HQS Macromolecules, Park, H. Baek, S. Park, I. Kong, D. Kim and W. Joo, Purification and biochemical characterization of a fibrinolytic enzyme from Bacillus subtilis BK World J. Marchesi and A. Dobson, Marine metagenomics: Strategies for the discovery of novel enzymes with biotechnological applications from marine environments. Cell Fact, Vol. J Ind Microbiol Biot. Yuan, J. Thrombolytic effects of Douchi fibrinolytic enzyme from Bacillus subtilis LD in vitro and in vivo.
Bmc Biotechnol. Collen, D. Lijnen, Tissue-type plasminogen activator: a historical perspective and personal account. J Thromb Haemost. Mine, Y. Fibrinolytic enzymes in Asian traditional fermented foods. Food Res Int. The biotechnological potential of fibrinolytic enzymes in the dissolution of endogenous blood thrombi. Biotechnol Progr. Duffy, M. Urokinase plasminogen activator and its inhibitor, PAI-1, as prognostic markers in breast cancer: from pilot to level I evidence studies.
Clin Chem. Moukhametova, L. Properties of the urokinase-type plasminogen activator modified with phenylglyoxal. Russ Bioorg Chem. Wei, X. Production of fibrinolytic enzyme from Bacillus amyloliquefaciens by fermentation of chickpeas, with the evaluation of the anticoagulant and antioxidant properties of chickpeas. J Agr Food Chem. Kim, S. Purification and characterization of a fibrinolytic subtilisin-like protease of Bacillus subtilis TP-6 from an Indonesian fermented soybean.
J Ind Microbio Biotech. Yao, Z. Properties of a fibrinolytic enzyme secreted by Bacillus amyloliquefaciens RSB34, isolated from Doenjang. J Microbio Biotech. Purification and partial characterization of serine fibrinolytic enzyme from Bacillus megaterium KSK isolated from Kishk , a traditional egyptian fermented food. Appl Biochem Micro. Suzuki, Y. Dietary supplementation with fermented soybeans suppresses intimal thickening. Wong, A. Novel fibrinolytic enzyme in fermented shrimp paste, a traditional Asian fermented seasoning. Chang, C.
Purification and biochemical properties of a fibrinolytic enzyme from Bacillus subtilis- fermented red bean. Food Chem. Peng, Y. Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from Douchi , a traditional Chinese soybean food. Comp Biochem Phys B. Zhang, R. Gene expression and characteristics of a novel fibrinolytic enzyme subtilisin DFE in Escherichia coli.
Lett Appl Microbiol. Jeon, H. Screening and characterization of potential Bacillus starter cultures for fermenting low-salt soybean paste Doenjang. J Microbiol Biotech. Jeong, S. Characterization of aprE, a fibrinolytic enzyme from Bacillus subtilis HK J Microbiol Biotechnol. Kurosawa, Y. A single-dose of oral nattokinase potentiates thrombolysis and anti-coagulation profiles. Sci Rep-UK. Urano, T. The profibrinolytic enzyme subtilisin NAT purified from Bacillus subtilis cleaves and inactivates plasminogen activator inhibitor type 1.
J Biol Chem. M Weng, Y. Nattokinase: an oral antithrombotic agent for the prevention of cardiovascular disease. Int J Mol Sci. Fujita, H. Fermented soybean-derived water-soluble Touchi extract inhibits alpha-glucosidase and is antiglycemic in rats and humans after single oral treatments. J Nutr.
Moreno, C. Polymorphism in repeated 16S rRNA genes is a common property of type strains and environmental isolates of the genus Vibrio. Astrup, T. The fibrin plate method for estimating fibrinolytic activity. Arch Biochem Bioph. Purification and characterization of subtilisin DJ-4 secreted by Bacillus sp.
Biosci Biotech Biochem. Purification and characterization of a novel fibrinolytic enzyme from chive Allium tuberosum. Food Sci Biotechnol.
Lu, X. Biotechnol Letters. Sumi, H. A novel fibrinolytic enzyme nattokinase in the vegetable cheese Natto ; a typical and popular soybean food in the Japanese diet.
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Zheng, Z. Construction of a 3D model of nattokinase, a novel fibrinolytic enzyme from Bacillus Natto - A novel nucleophilic catalytic mechanism for nattokinase. J Mol Graph Model.
Ahn, M. Characterization of a novel fibrinolytic enzyme, BsfA , from Bacillus subtili s ZA in Kimchi reveals its pertinence to thrombosis treatment. Ko, J. Identification of two novel fibrinolytic enzymes from Bacillus subtilis QK Comp Biochem Phys C. Nakamura, T. Nucleotide sequence of the subtilisin NAT.