Isolation, production, purification, assay and characterization of fibrinolytic enzymes (Nattokinase, Streptokinase and Urokinase) from bacterial sources

African Journal of Biotechnology

Volumn 10, Issue 8, 2011, Pages 1408-1420

  Dubey, R ^a   Kumar, J ^a   Agrawala, D ^a   Char, T ^a   Pusp, P ^a  

^a Galaxy Concepts Pvt Limited   (India)

Author keywords

Anticoagulant activity; Casein; Edman degradation; Enzyme screening; Enzyme thermodynamics; Expression system; Fibrinolytic enzyme activity; Haemolytic activity; Protein fraction precipitation; Serum and plasminogen plate technique; Submerge fermentation; Zymography

Indexed keywords

CASEIN; FIBRINOLYTIC AGENT; GENOMIC DNA; NATTOKINASE; STREPTOKINASE; UNCLASSIFIED DRUG; UROKINASE;

ARTICLE; BACILLUS SUBTILIS; BACTERIAL STRAIN; BACTERIUM CULTURE; BETA HEMOLYTIC STREPTOCOCCUS; CONTROLLED STUDY; DNA FRAGMENTATION; DRUG ISOLATION; DRUG PURIFICATION; DRUG SCREENING; DRUG SYNTHESIS; ESCHERICHIA COLI; FIBRINOLYSIS; HYDROPHILICITY; MOLECULAR WEIGHT; NONHUMAN; PH; PROTEIN DEGRADATION; PSEUDOMONAS; TEMPERATURE SENSITIVITY;

BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); PSEUDOMONAS SP.;

EID: 79952161313     PISSN: 16845315     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (17)

1. Adinarayana K, Bhavani DR, Poluri E, Tadimallo P, Vinjamuri S (2008). Urokinase- a strong plaminogen activator. Biotechnol. Mol. Biol. Rev. 3: 058-070
2. Banerjee A, Chistic Y, Banerjee UC (2004). Streptokinase, a clinically useful thrombolytic agent. Biotechnol. Adv. 22: 287-305
3. Bernik MB, Oller EP (1973). Increase plasminogen activator (Urokinase) in tissue culture after fibrin deposition. J.Clin Invest.52:823-834
4. Chitte RR, Dey S (2000). Potent fibrinolytic enzyme from a thermophilic Streptomyces megasporus strain SD 5. Lett. Appl. Microbiol. 31: 405- 410.
5. Endrogan E, Ozer AY, Volkan B, Caner B, Bilgili H (2006). Thrombus localization by using streptokinase containing vesicular system. Drug Deliv. 13: 303-309
6. Fujita M, Hong K, Ito Y, Fujii R, Kariya K, Nishimuro S. (1995). Thrombolytic effect of Nattokinase on a chemically induced thrombosis model in rat. Biol. Pharm. Bull. 18:1387-1391
7. Jian Sha CL, Galindo V, Pancholi VL, Popov Y, Zhao CWH, Chopra AK (2003). Differential expression of the enolase gene under in vivo versus in vitro growth conditions of Aeromonas hydrophila. Microbial pathogenesis, 34: 195-204
8. Kim DM, Lee SJ, Kim IC, Kim ST, Byun SM (2000). Asp14-His48 region of streptokinase is important in binding to substrate plasminogen. Thromb Res. 99: 93-98
9. Kunamneni A, Ravuri BD, Saisha V, Ellaiah P, Prabhakhar T (2008). Urokinase-a very popular cardiovascular agent. Recent patent cardiovas Drug Disc. 3: 45-58
10. Mohammad B, Hossein M, Mohammad R (2009). Production and purification of streptokinase by protected affinity chromatography. Avicenna J. Med. Biotechnol. 1: 47-51
11. Nakamura T, Yamagata Y, Ichishima E (1992). Nucleotide sequence of the subtilisin NAT gene, aprN, of Bacillus subtilis (natto). Biosci. Biotechnol. Biochem. 56: 1869-1871
12. Sumi H, Hamada H, Nakanishi K, Hiratani H (1990). Enhancement of the fibrinolytic activity in plasma by oral administration of Nattokinase. Acta Haematol. 84: 139-143
13. Uversky VN, Fink AL (2004). Conformational constraints for amyloid fibrillation: The importance of being unfolded Biochem. Biophys. Acta, 1698: 131-153
14. Viles-Gonzalez JF, Fuster V, Badimon JJ (2004). Atherothrombosis: A widespread disease with unpredictable and life-threatening consequences. Eur. Heart J. 25: 1197-1207
15. Walker JE, Ogstron D (1982). The inhibition of tissue activator and urokinase by human plasma. Thromb Haemost; 47:265.
16. Wang X, Lin X, Loy JA, Tang J, Zhang XC (1998). Crystal structure of the catalytic domain of human plasmin complexed with streptokinase. Science, 282:1662-1665
17. Yoshinori M, Ada HKW, Jiang B (2005). Fibrinolytic enzymes in traditional fermented food. Food Res. In. 38:243-250