Streptokinase: An Efficient Enzyme in Cardiac Medicine

Author(s): Muhammad A. Zia*

Journal Name: Protein & Peptide Letters

Volume 27 , Issue 2 , 2020


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Graphical Abstract:


Abstract:

An imbalance in oxygen supply to cardiac tissues or formation of thrombus leads to deleterious results like pulmonary embolism, coronary heart disease and acute cardiac failure. The formation of thrombus requires clinical encounter with fibrinolytic agents including streptokinase, urokinase or tissue plasminogen activator. Irrespective to urokinase and tissue plasminogen activator, streptokinase is still a significant agent in treatment of cardiovascular diseases. Streptokinase, being so economical, has an important value in treating cardiac diseases in developing countries. This review paper will provide the maximum information to enlighten all the pros and cons of streptokinase up till now. It has been concluded that recent advances in structural/synthetic biology improved SK with enhanced half-life and least antigenicity. Such enzyme preparations would be the best thrombolytic agents.

Keywords: Streptokinase, Streptococci, thrombolytic agent, drug, myocardial infarction, fibrinolytic agents.

[1]
Mendis, S.; Lindholm, L.H.; Anderson, S.G.; Alwan, A.; Koju, R.; Onwubere, B.J.C.; Kayani, A.M.; Abeysinghe, N.; Duneas, A.; Tabagari, S.; Fan, W.; Sarraf-Zadegan, N.; Nordet, P.; Whitworth, J.; Heagerty, A. Total cardiovascular risk approach to improve efficiency of cardiovascular prevention in resource constrain settings. J. Clin. Epidemiol., 2011, 64(12), 1451-1462.
[http://dx.doi.org/10.1016/j.jclinepi.2011.02.001] [PMID: 21530172]
[2]
Murray, C.J.; Lopez, A.D. Mortality by cause for eight regions of the world: Global burden of disease study. Lancet, 1997, 349(9061), 1269-1276.
[http://dx.doi.org/10.1016/S0140-6736(96)07493-4] [PMID: 9142060]
[3]
Francis, C.W.; Marder, V.J. Fibrinolytic therapy for venous thrombosis. Prog. Cardiovasc. Dis., 1991, 34(3), 193-204.
[http://dx.doi.org/10.1016/0033-0620(91)90013-C] [PMID: 1947124]
[4]
Konstantinides, S.; Goldhaber, S.Z. Pulmonary embolism: Risk assessment and management. Eur. Heart J., 2012, 33(24), 3014-3022.
[http://dx.doi.org/10.1093/eurheartj/ehs258] [PMID: 22961946]
[5]
Banerjee, A.; Chisti, Y.; Banerjee, U.C. Streptokinase--a clinically useful thrombolytic agent. Biotechnol. Adv., 2004, 22(4), 287-307.
[http://dx.doi.org/10.1016/j.biotechadv.2003.09.004] [PMID: 14697452]
[6]
Arshad, A.; Zia, M.A.; Asgher, M.; Joyia, F.A.; Arif, M. Enhanced production of streptokinase from Streptococcus agalactiae EBL-31 by response surface methodology. Pak. J. Pharm. Sci., 2018, 31(4), 1597-1602.
[PMID: 30058554]
[7]
Menon, V.; Harrington, R.A.; Hochman, J.S.; Cannon, C.P.; Goodman, S.D.; Wilcox, R.G.; Schünemann, H.J.; Ohman, E.M. Thrombolysis and adjunctive therapy in acute myocardial infarction: The Seventh ACCP Conference on Antithrombotic and Thrombolytic Therapy. Chest, 2004, 126(3)(Suppl.), 549S-575S.
[http://dx.doi.org/10.1378/chest.126.3_suppl.549S] [PMID: 15383484]
[8]
Wong, S.L.; Ye, R.; Nathoo, S. Engineering and production of streptokinase in a Bacillus subtilis expression-secretion system. Appl. Environ. Microbiol., 1994, 60(2), 517-523.
[PMID: 8135514]
[9]
Kim, D.M.; Lee, S.J.; Kim, I.C.; Kim, S.T.; Byun, S.M. Asp41-His48 region of streptokinase is important in binding to a substrate plasminogen. Thromb. Res., 2000, 99(1), 93-98.
[http://dx.doi.org/10.1016/S0049-3848(00)00225-5] [PMID: 10904106]
[10]
Long-term effects of intravenous thrombolysis in acute myocardial infarction: Final report of the GISSI study. Gruppo Italiano per lo Studio della Streptochi-nasi nell’Infarto Miocardico (GISSI). Lancet, 1987, 2(8564), 871-874.
[PMID: 2889079]
[11]
Bade, A.S.; Shaikh, S.S.A.; Khemani, H.; Singh, G.; Bansal, N.O. Thrombolysis is an effective and safe therapy in stuck mitral valves with delayed presentation as well as hemodynamically unstable patients: A single centre study. Cardiol. Res., 2018, 9(3), 161-164.
[http://dx.doi.org/10.14740/cr708w] [PMID: 29904451]
[12]
Faran, G.; Zia, M.A.; Shahid, M.; Abdullah, S. Improved streptokinase production; UV irradiation of Streptococcus equisimilis. Prof. Med. J., 2015, 22(5), 656-663.
[13]
Arabi, R.; Roohvand, F.; Norouzian, D.; Sardari, S.; Aghasadeghi, M.R.; Khanahmad, H.; Memarnejadian, A.; Motevalli, F. A comparative study on the activity and antigenicity of truncated and full-length forms of streptokinase. Pol. J. Microbiol., 2011, 60(3), 243-251.
[PMID: 22184932]
[14]
Cornu, C.; Boutitie, F.; Candelise, L.; Boissel, J.P.; Donnan, G.A.; Hommel, M.; Jaillard, A.; Lees, K.R. Streptokinase in acute ischemic stroke: An individual patient data meta-analysis: the thrombolysis in acute stroke pooling project. Stroke, 2000, 31(7), 1555-1560.
[http://dx.doi.org/10.1161/01.STR.31.7.1555] [PMID: 10884453]
[15]
Sikri, N.; Bardia, A. A history of streptokinase use in acute myocardial infarction. Tex. Heart Inst. J., 2007, 34(3), 318-327.
[PMID: 17948083]
[16]
Zia, M.A.; Faisal, R.; Abbas, R.Z.; Faran, G.E.; Saleemi, M.; Khan, J.A. Comparison of streptokinase activity from Streptococcus mutans using different substrates Pak. Vet. J., 2013, 33(1), 77-79.
[17]
Quintero, L.; Hernández, F.; Acelia, M.; María, C.; López, M.; Barcelona, S.; Ibargollín, R.; Bobillo, H.; Aguilera, A.; Bermúdez, Y. Initial Evidence of safety and clinical effect of recombinant streptokinase suppository in acute hemorrhoidal disease. Open, Proof-of-Concept. Pilot Trial. Biotecnol. Apl., 2010, 27(4), 277-280.
[18]
Kunamneni, A.; Abdelghani, T.T.A.; Ellaiah, P. Streptokinase--the drug of choice for thrombolytic therapy. J. Thromb. Thrombolysis, 2007, 23(1), 9-23.
[http://dx.doi.org/10.1007/s11239-006-9011-x] [PMID: 17111203]
[19]
Christensen, L.R. Streptococcal fibrinolysis: A proteolytic reaction due to a serum enzyme activated by Streptococcal fibrinolysin. J. Gen. Physiol., 1945, 28(4), 363-383.
[http://dx.doi.org/10.1085/jgp.28.4.363] [PMID: 19873427]
[20]
Sherry, S. The fibrinolytic activity of streptokinase activated human plasmin. J. Clin. Invest., 1954, 33(7), 1054-1063.
[http://dx.doi.org/10.1172/JCI102973] [PMID: 13174663]
[21]
Tillett, W.S.; Johnson, A.J. McCARTY, W.R. The intravenous infusion of the streptococcal fibrinolytic principle (streptokinase) into patients. J. Clin. Invest., 1955, 34(2), 169-185.
[http://dx.doi.org/10.1172/JCI103071] [PMID: 13233340]
[22]
Ruegsegger, P.; Nydick, I.; Hutter, R.C.; Freiman, A.H.; Bang, N.U.; Cliffton, E.E.; Ladue, J.S. Fibrinolytic (plasmin) therapy of experimental coronary thrombi with alteration of the evolution of myocardial infarction. Circulation, 1959, 19(1), 7-13.
[http://dx.doi.org/10.1161/01.CIR.19.1.7] [PMID: 13619015]
[23]
Schmutzler, R.; Heckner, F.; Körtge, P.; van de Loo, J.; Poliwoda, H.; Pezold, F. A.; Praetorius, F.; Zekorn, D. On thrombolytic therapy of a recent myocardial infarct. I. Introduction, treatment plans, general clinical results. Dtsch. Med. Wochenschr. 1946, 1966, 91(13), 581-587.
[http://dx.doi.org/10.1055/s-0028-1110619]
[24]
Rentrop, P.; Blanke, H.; Karsch, K. R.; Wiegand, V.; Köstering, H.; Rahlf, G.; Oster, H.; Leitz, K. Reopening of infarct-occluded vessel by transluminal recanalisation and intracoronary streptokinase application. Dtsch. Med. Wochenschr. 1946, 1979, 104(41), 1438-1440.
[http://dx.doi.org/10.1055/s-0028-1129117.]
[25]
Laffel, G.L.; Braunwald, E. Thrombolytic therapy. A new strategy for the treatment of acute myocardial infarction (2). N. Engl. J. Med., 1984, 311(12), 770-776.
[http://dx.doi.org/10.1056/NEJM198409203111205] [PMID: 6236369]
[26]
Marx, M.; Levin, D.C. Coronary thrombolytic therapy: State of the art. AJR Am. J. Roentgenol., 1986, 147(1), 1-8.
[http://dx.doi.org/10.2214/ajr.147.1.1] [PMID: 3521234]
[27]
Klugmann, S.; Della Grazia, E.; Maras, P.; Medugno, G.; Pandullo, C.; Salvi, A.; Camerini, F. Problems appearing after pharmacologic thrombolysis in acute myocardial infarct. G. Ital. Cardiol., 1983, 13(4), 353-356.
[PMID: 6884679]
[28]
Verheugt, F.W.; van Eenige, M.J.; Res, J.C.; Simoons, M.L.; Serruys, P.W.; Vermeer, F.; van Hoogenhuyze, D.C.; Remme, P.J.; de Zwaan, C.; Baer, F. Bleeding complications of intracoronary fibrinolytic therapy in acute myocardial infarction. Assessment of risk in a randomised trial. Br. Heart J., 1985, 54(5), 455-459.
[http://dx.doi.org/10.1136/hrt.54.5.455] [PMID: 3902068]
[29]
Vermeer, F.; Simoons, M.L.; Bär, F.W.; Tijssen, J.G.; van Domburg, R.T.; Serruys, P.W.; Verheugt, F.W.; Res, J.C.; de Zwaan, C.; van der Laarse, A. Which patients benefit most from early thrombolytic therapy with intracoronary streptokinase? Circulation, 1986, 74(6), 1379-1389.
[http://dx.doi.org/10.1161/01.CIR.74.6.1379] [PMID: 3779921]
[30]
Diwedi, S.K.; Hiremath, J.S.; Kerkar, P.G.; Reddy, K.N.; Manjunath, C.N.; Ramesh, S.S.; Prabhavati, S.; Dhobe, M.; Singh, K.; Bhusari, P.; Rao, R. Indigenous recombinant streptokinase vs natural streptokinase in acute myocardial infarction patients: Phase III multicentric randomized double blind trial. Indian J. Med. Sci., 2005, 59(5), 200-207.
[http://dx.doi.org/10.4103/0019-5359.16256] [PMID: 15985728]
[31]
Babu, V.; Subathra Devi, C. In vitro thrombolytic activity of purified streptokinase extracted from Streptococcus equinus VIT_VB2 isolated from bovine milk. J. Thromb. Thrombolysis, 2015, 39(1), 71-78.
[http://dx.doi.org/10.1007/s11239-014-1093-2] [PMID: 24897956]
[32]
Wang, X.; Tang, J.; Hunter, B.; Zhang, X.C. Crystal structure of streptokinase beta-domain. FEBS Lett., 1999, 459(1), 85-89.
[http://dx.doi.org/10.1016/S0014-5793(99)01214-4] [PMID: 10508922]
[33]
Nihalani, D.; Sahni, G. Streptokinase contains two independent plasminogen-binding sites. Biochem. Biophys. Res. Commun., 1995, 217(3), 1245-1254.
[http://dx.doi.org/10.1006/bbrc.1995.2902] [PMID: 8554583]
[34]
Beldarraín, A.; López-Lacomba, J.L.; Kutyshenko, V.P.; Serrano, R.; Cortijo, M. Multidomain structure of a recombinant streptokinase. A differential scanning calorimetry study. J. Protein Chem., 2001, 20(1), 9-17.
[http://dx.doi.org/10.1023/A:1011044718840] [PMID: 11330353]
[35]
Vaishnavi, B.; Subathra Devi, C. Potential application of immobilized streptokinase extracted from Streptococcus equinus VIT_VB2. Prep. Biochem. Biotechnol., 2017, 47(10), 1032-1036.
[http://dx.doi.org/10.1080/10826068.2017.1373291] [PMID: 29020506]
[36]
Rijal, K.R.; Dhakal, N.; Shah, R.C.; Timilsina, S.; Mahato, P.; Thapa, S.; Ghimire, P. Antibiotic susceptibility of group A Streptococcus isolated from throat swab culture of school children in Pokhara, Nepal. Nepal Med. Coll. J., 2009, 11(4), 238-240.
[PMID: 20635601]
[37]
Kumar, S. Bioremediation of chlorpyrifos by bacteria isolated from the cultivated soils. Int. J. Pharma Bio Sci., 2011, 2(3), 359-366.
[38]
Malke, H.; Roe, B.; Ferretti, J.J. Nucleotide sequence of the streptokinase gene from Streptococcus equisimilis H46A. Gene, 1985, 34(2-3), 357-362.
[http://dx.doi.org/10.1016/0378-1119(85)90145-3] [PMID: 2989113]
[39]
Gase, K.; Ellinger, T.; Malke, H. Complex transcriptional control of the streptokinase gene of Streptococcus equisimilis H46A. Mol. Gen. Genet., 1995, 247(6), 749-758.
[http://dx.doi.org/10.1007/BF00290407] [PMID: 7616967]
[40]
Bernheimer, A.W. Formation of a bacterial toxin (streptolysin S) by resting cells. J. Exp. Med., 1949, 90(5), 373-392.
[http://dx.doi.org/10.1084/jem.90.5.373] [PMID: 18143584]
[41]
Babashamsi, M.; Razavian, M.H.; Nejadmoghaddam, M.R. Production and purification of streptokinase by protected affinity chromatography. Avicenna J. Med. Biotechnol., 2009, 1(1), 47-51.
[PMID: 23407807]
[42]
Dubey, R.; Kumar, J.; Agrawala, D.; Char, T.; Pusp, P. Isolation, production, purification, assay and characterization of fibrinolytic enzymes (Nattokinase, Streptokinase and Urokinase) from bacterial sources. Afr. J. Biotechnol., 2013, 10(8), 1408-1420.
[http://dx.doi.org/10.4314/ajb.v10i8]
[43]
Höfling, B.; von Pölnitz, A. Invasive strategy for treatment of myocardial infarction. J. Cardiovasc. Pharmacol., 1990, 16(Suppl. 5), S120-S122.
[http://dx.doi.org/10.1097/00005344-199006165-00021] [PMID: 11527114]
[44]
Holmström, B. Production of streptokinase in continuous culture. Appl. Microbiol., 1968, 16(1), 73-77.
[PMID: 4865907]
[45]
Ellis, R.P.; Armstrong, C.H. Production of capsules, streptokinase, and streptodornase by Streptococcus group E. Am. J. Vet. Res., 1971, 32(2), 349-356.
[PMID: 5545466]
[46]
Fratantoni, J.C.; Ness, P.; Simon, T.L. Thrombolytic therapy: current status. N. Engl. J. Med., 1975, 293(21), 1073-1078.
[http://dx.doi.org/10.1056/NEJM197511202932106] [PMID: 1178024]
[47]
McCoy, H.E.; Broder, C.C.; Lottenberg, R. Streptokinases produced by pathogenic group C streptococci demonstrate species-specific plasminogen activation. J. Infect. Dis., 1991, 164(3), 515-521.
[http://dx.doi.org/10.1093/infdis/164.3.515] [PMID: 1869838]
[48]
Estrada, M.P.; Hernández, L.; Pérez, A.; Rodríguez, P.; Serrano, R.; Rubiera, R.; Pedraza, A.; Padrón, G.; Antuch, W.; de la Fuente, J. High level expression of streptokinase in Escherichia coli. Biotechnology (N. Y.), 1992, 10(10), 1138-1142.
[PMID: 1368792]
[49]
Malke, H.; Steiner, K.; Gase, K.; Frank, C. Expression and regulation of the streptokinase gene. Methods, 2000, 21(2), 111-124.
[http://dx.doi.org/10.1006/meth.2000.0982] [PMID: 10816372]
[50]
Yazdani, S.S.; Shakri, A.R.; Chitnis, C.E. A high cell density fermentation strategy to produce recombinant malarial antigen in E. coli. Biotechnol. Lett., 2004, 26(24), 1891-1895.
[http://dx.doi.org/10.1007/s10529-004-6040-4] [PMID: 15672234]
[51]
Mukherjee, P.; Leman, L.J.; Griffin, J.H.; Ghadiri, M.R. Design of a DNA-programmed plasminogen activator. J. Am. Chem. Soc., 2018, 140(45), 15516-15524.
[http://dx.doi.org/10.1021/jacs.8b10166] [PMID: 30347143]
[52]
Baneyx, F.; Mujacic, M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol., 2004, 22(11), 1399-1408.
[http://dx.doi.org/10.1038/nbt1029] [PMID: 15529165]
[53]
Castellino, F.J. Recent advances in the chemistry of the fibrinolytic system. Chem. Rev., 1981, 81(5), 431-446.
[http://dx.doi.org/10.1021/cr00045a001]
[54]
Shi, G.Y.; Chang, B.I.; Su, S.W.; Young, K.C.; Wu, D.H.; Chang, L.C.; Tsai, Y.S.; Wu, H.L. Preparation of a novel streptokinase mutant with improved stability. Thromb. Haemost., 1998, 79(5), 992-997.
[http://dx.doi.org/10.1055/s-0037-1615108] [PMID: 9609235]
[55]
Dundar, Y.; Hill, R.; Dickson, R.; Walley, T. Comparative efficacy of thrombolytics in acute myocardial infarction: A systematic review. QJM, 2003, 96(2), 103-113.
[http://dx.doi.org/10.1093/qjmed/hcg016] [PMID: 12589008]
[56]
Jackson, K.W.; Tang, J. Complete amino acid sequence of streptokinase and its homology with serine proteases. Biochemistry, 1982, 21(26), 6620-6625.
[http://dx.doi.org/10.1021/bi00269a001] [PMID: 6760891]
[57]
Castellino, F.J.; Sodetz, J.M.; Brockway, W.J.; Siefring, G.E. Jr Streptokinase. Methods Enzymol., 1976, 45, 244-257.
[http://dx.doi.org/10.1016/S0076-6879(76)45024-3] [PMID: 1011996]
[58]
Malke, H.; Ferretti, J.J. Streptokinase: Cloning, expression, and excretion by Escherichia coli. Proc. Natl. Acad. Sci. USA, 1984, 81(11), 3557-3561.
[http://dx.doi.org/10.1073/pnas.81.11.3557] [PMID: 6374659]
[59]
Avilán, L.; Yarzábal, A.; Jürgensen, C.; Bastidas, M.; Cruz, J.; Puig, J. Cloning, expression and purification of recombinant streptokinase: Partial characterization of the protein expressed in Escherichia coli. Braz. J. Med. Biol. Res., 1997, 30(12), 1427-1430.
[http://dx.doi.org/10.1590/S0100-879X1997001200007] [PMID: 9686161]
[60]
Balagurunathan, B.; Jayaraman, G. Theoretical and experimental investigation of chaperone effects on soluble recombinant proteins in Escherichia coli: Effect of free DnaK level on temperature-induced recombinant streptokinase production. Syst. Synth. Biol., 2008, 2(1-2), 27-48.
[http://dx.doi.org/10.1007/s11693-009-9021-z] [PMID: 19169848]
[61]
Goyal, D.; Sahni, G.; Sahoo, D.K. Enhanced production of recombinant streptokinase in Escherichia coli using fed-batch culture. Bioresour. Technol., 2009, 100(19), 4468-4474.
[http://dx.doi.org/10.1016/j.biortech.2009.04.008] [PMID: 19428239]
[62]
Babu, V.; Subathra Devi, C. Exploring the in vitro thrombolytic potential of streptokinase-producing β-hemolytic Streptococci isolated from bovine milk. J. Gen. Appl. Microbiol., 2015, 61(4), 139-146.
[http://dx.doi.org/10.2323/jgam.61.139] [PMID: 26377134]
[63]
Nguyen, S.T.; Quyen, D.T.; Vu, H.D. Highly effective renaturation of a streptokinase from Streptococcus pyogenes DT7 as inclusion bodies overexpressed in Escherichia coli. BioMed Res. Int., 2014. 2014324705
[http://dx.doi.org/10.1155/2014/324705] [PMID: 24883307]
[64]
Taheri, M.N.; Behzad-Behbahani, A.; Rafiei Dehbidi, G.; Salehi, S.; Sharifzadeh, S. Engineering, expression and purification of a chimeric fibrin-specific streptokinase. Protein Expr. Purif., 2016, 128, 14-21.
[http://dx.doi.org/10.1016/j.pep.2016.08.003] [PMID: 27496727]
[65]
Laplace, F.; Müller, J.; Gumpert, J.; Malke, H. Novel shuttle vectors for improved streptokinase expression in streptococci and bacterial L-forms. FEMS Microbiol. Lett., 1989, 53(1-2), 89-94.
[http://dx.doi.org/10.1111/j.1574-6968.1989.tb03602.x] [PMID: 2693202]
[66]
Jackson, K.W.; Malke, H.; Gerlach, D.; Ferretti, J.J.; Tang, J. Active streptokinase from the cloned gene in Streptococcus sanguis is without the carboxyl-terminal 32 residues. Biochemistry, 1986, 25(1), 108-114.
[http://dx.doi.org/10.1021/bi00349a016] [PMID: 3954985]
[67]
Klessen, C.; Malke, H. Expression of the streptokinase gene from Streptococcus equisimilis in Bacillus subtilis. J. Basic Microbiol., 1986, 26(2), 75-81.
[http://dx.doi.org/10.1002/jobm.3620260203] [PMID: 3090231]
[68]
Wu, X-C.; Ye, R.; Duan, Y.; Wong, S-L. Engineering of plasmin-resistant forms of streptokinase and their production in Bacillus subtilis: Streptokinase with longer functional half-life. Appl. Environ. Microbiol., 1998, 64(3), 824-829.
[PMID: 9501422]
[69]
Pimienta, E.; Ayala, J.C.; Rodríguez, C.; Ramos, A.; Van Mellaert, L.; Vallín, C.; Anné, J. Recombinant production of Streptococcus equisimilis streptokinase by Streptomyces lividans. Microb. Cell Fact., 2007, 6, 20.
[http://dx.doi.org/10.1186/1475-2859-6-20] [PMID: 17610745]
[70]
Yao, C-T.; Wu, J-M.; Liu, C-C.; Wu, M-H.; Chuang, H-Y.; Wang, J-N. Treatment of complicated parapneumonic pleural effusion with intrapleural streptokinase in children. Chest, 2004, 125(2), 566-571.
[http://dx.doi.org/10.1378/chest.125.2.566] [PMID: 14769739]
[71]
Gadalla, S.M.; Wang, T.; Haagenson, M.; Spellman, S.R.; Lee, S.J.; Williams, K.M.; Wong, J.Y.; De Vivo, I.; Savage, S.A. Association between donor leukocyte telomere length and survival after unrelated allogeneic hematopoietic cell transplantation for severe aplastic anemia. JAMA, 2015, 313(6), 594-602.
[http://dx.doi.org/10.1001/jama.2015.7] [PMID: 25668263]
[72]
Pratap, J.; Rajamohan, G.; Dikshit, K.L. Characteristics of glycosylated streptokinase secreted from Pichia pastoris: Enhanced resistance of SK to proteolysis by glycosylation. Appl. Microbiol. Biotechnol., 2000, 53(4), 469-475.
[http://dx.doi.org/10.1007/s002530051643] [PMID: 10803905]
[73]
Vellanki, R.N.; Potumarthi, R.; Mangamoori, L.N. Constitutive expression and optimization of nutrients for streptokinase production by Pichia pastoris using statistical methods. Appl. Biochem. Biotechnol., 2009, 158(1), 25-40.
[http://dx.doi.org/10.1007/s12010-008-8315-z] [PMID: 18654742]
[74]
Adivitiya, B.; Dagar, V.K.; Devi, N.; Khasa, Y.P. High level production of active streptokinase in Pichia pastoris fed-batch culture. Int. J. Biol. Macromol., 2016, 83, 50-60.
[http://dx.doi.org/10.1016/j.ijbiomac.2015.11.062] [PMID: 26631635]
[75]
Babbal, A.; Mohanty, S.; Khasa, Y.P. Engineering of deglycosylated and plasmin resistant variants of recombinant streptokinase in Pichia pastoris. Appl. Microbiol. Biotechnol., 2018, 102(24), 10561-10577.
[http://dx.doi.org/10.1007/s00253-018-9402-x] [PMID: 30298450]
[76]
Fantes, P.A.; Hoffman, C.S. A Brief History of Schizosaccharomyces pombe research: A perspective over the past 70 years. Genetics, 2016, 203(2), 621-629.
[http://dx.doi.org/10.1534/genetics.116.189407] [PMID: 27270696]
[77]
Kumar, R.; Singh, J. Biosimilar drugs: Current status. Int. J. Appl. Basic Med. Res., 2014, 4(2), 63-66.
[http://dx.doi.org/10.4103/2229-516X.136774] [PMID: 25143877]
[78]
Goffeau, A.; Barrell, B.G.; Bussey, H.; Davis, R.W.; Dujon, B.; Feldmann, H.; Galibert, F.; Hoheisel, J.D.; Jacq, C.; Johnston, M.; Louis, E.J.; Mewes, H.W.; Murakami, Y.; Philippsen, P.; Tettelin, H.; Oliver, S.G. Life with 6000 genes. Science, 1996, 274(5257), 546-563-567.
[http://dx.doi.org/10.1126/science.274.5287.546] [PMID: 8849441]
[79]
Burgenson, D.; Gurramkonda, C.; Pilli, M.; Ge, X.; Andar, A.; Kostov, Y.; Tolosa, L.; Rao, G. Rapid recombinant protein expression in cell-free extracts from human blood. Sci. Rep., 2018, 8(1), 9569.
[http://dx.doi.org/10.1038/s41598-018-27846-8] [PMID: 29934577]
[80]
Timm, A.C.; Shankles, P.G.; Foster, C.M.; Doktycz, M.J.; Retterer, S.T. Toward microfluidic reactors for cell-free protein synthesis at the point-of-care. Small, 2016, 12(6), 810-817.
[http://dx.doi.org/10.1002/smll.201502764] [PMID: 26690885]
[81]
Jackson, K.; Jin, S.; Fan, Z.H. Optimization of a miniaturized fluid array device for cell-free protein synthesis. Biotechnol. Bioeng., 2015, 112(12), 2459-2467.
[http://dx.doi.org/10.1002/bit.25668] [PMID: 26037852]
[82]
Martin, R.W.; Majewska, N.I.; Chen, C.X.; Albanetti, T.E.; Jimenez, R.B.C.; Schmelzer, A.E.; Jewett, M.C.; Roy, V. Development of a CHO-based cell-free platform for synthesis of active monoclonal antibodies. ACS Synth. Biol., 2017, 6(7), 1370-1379.
[http://dx.doi.org/10.1021/acssynbio.7b00001] [PMID: 28350472]
[83]
Tran, K.; Gurramkonda, C.; Cooper, M.A.; Pilli, M.; Taris, J.E.; Selock, N.; Han, T-C.; Tolosa, M.; Zuber, A.; Peñalber-Johnstone, C.; Dinkins, C.; Pezeshk, N.; Kostov, Y.; Frey, D.D.; Tolosa, L.; Wood, D.W.; Rao, G. Cell-free production of a therapeutic protein: Expression, purification, and characterization of recombinant streptokinase using a CHO lysate. Biotechnol. Bioeng., 2018, 115(1), 92-102.
[http://dx.doi.org/10.1002/bit.26439] [PMID: 28843001]
[84]
Khan, M.S.; Mustafa, G.; Joyia, F.A. Enzymes: Plant-based production and their applications. Protein Pept. Lett., 2018, 25(2), 136-147.
[http://dx.doi.org/10.2174/0929866525666180122123722] [PMID: 29359656]
[85]
Boulaflous, A.; Saint-Jore-Dupas, C.; Herranz-Gordo, M-C.; Pagny-Salehabadi, S.; Plasson, C.; Garidou, F.; Kiefer-Meyer, M-C.; Ritzenthaler, C.; Faye, L.; Gomord, V. Cytosolic N-terminal arginine-based signals together with a luminal signal target a type II membrane protein to the plant ER. BMC Plant Biol., 2009, 9, 144.
[http://dx.doi.org/10.1186/1471-2229-9-144] [PMID: 19995436]
[86]
Reggi, S.; Marchetti, S.; Patti, T.; De Amicis, F.; Cariati, R.; Bembi, B.; Fogher, C. Recombinant human acid beta-glucosidase stored in tobacco seed is stable, active and taken up by human fibroblasts. Plant Mol. Biol., 2005, 57(1), 101-113.
[http://dx.doi.org/10.1007/s11103-004-6832-x] [PMID: 15821871]
[87]
Khan, M.S. Biopharming: A biosecurity measure to combat newcastle disease for household food security. Biosafety (Los Angel.), 2015, 04(01)
[http://dx.doi.org/10.4172/2167-0331.1000e156]
[88]
Daniell, H.; Khan, M.S.; Allison, L. Milestones in chloroplast genetic engineering: An environmentally friendly era in biotechnology. Trends Plant Sci., 2002, 7(2), 84-91.
[http://dx.doi.org/10.1016/S1360-1385(01)02193-8] [PMID: 11832280]
[89]
Fischer, B.B.; Krieger-Liszkay, A.; Eggen, R.L. Photosensitizers neutral red (type I) and rose bengal (type II) cause light-dependent toxicity in Chlamydomonas reinhardtii and induce the Gpxh gene via increased singlet oxygen formation. Environ. Sci. Technol., 2004, 38(23), 6307-6313.
[http://dx.doi.org/10.1021/es049673y] [PMID: 15597886]
[90]
Satoskar, A.R.; Okano, M.; Connaughton, S.; Raisanen-Sokolwski, A.; David, J.R.; Labow, M. Enhanced Th2-like responses in IL-1 type 1 receptor-deficient mice. Eur. J. Immunol., 1998, 28(7), 2066-2074.
[http://dx.doi.org/10.1002/(SICI)1521-4141(199807)28:07<2066: AID-IMMU2066>3.0.CO;2-X] [PMID: 9692874]
[91]
Hermentin, P.; Cuesta-Linker, T.; Weisse, J.; Schmidt, K-H.; Knorst, M.; Scheld, M.; Thimme, M. Comparative analysis of the activity and content of different streptokinase preparations. Eur. Heart J., 2005, 26(9), 933-940.
[http://dx.doi.org/10.1093/eurheartj/ehi093] [PMID: 15637085]
[92]
Rouf, S.A.; Moo-Young, M.; Chisti, Y. Tissue-type plasminogen activator: characteristics, applications and production technology. Biotechnol. Adv., 1996, 14(3), 239-266.
[http://dx.doi.org/10.1016/0734-9750(96)00019-5] [PMID: 14537155]


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VOLUME: 27
ISSUE: 2
Year: 2020
Published on: 14 October, 2019
Page: [111 - 119]
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DOI: 10.2174/0929866526666191014150408
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