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Role of Streptokinase as a Thrombolytic Agent for Medical Applications
Published in Pankaj Bhatt, Industrial Applications of Microbial Enzymes, 2023
Hamza Rafeeq, Muhammad Anjum Zia, Asim Hussain, Ayesha Safdar, Muhammad Bilal, Hafiz M. N. Iqbal
It is an extracellular enzyme produced by different strains of beta-hemolytic streptococci. Streptokinase is the protease, which consists of single-chain polypeptide and performs the function of activating plasminogen in blood circulation. Its molecular weight is 45–50 kDa (Tadayon et al., 2015), and it contains 414 amino acids, having isoelectric pH 7.3–7.6. It shows maximum activity at pH 7.5 (Chapurina et al., 2016). Streptokinase does not contain compounds such as cysteine, phosphorus, lipids, and carbohydrates. There is a great difference between the structure of streptokinase produced by different strains of cocci (Basak et al., 2016). In 1982, two scientists named Jackson and Tang reported the whole sequence of amino acids of streptokinase that also shows the difference in structure (Huish et al., 2017). Contrasting other fibrinolytic agents, streptokinase does not show its own proteolytic activity. It activates the plasminogen as it forms the complex with plasminogen. Streptokinase plasminogen complex activates the other free proenzymes molecule plasminogen into proteolytic plasmin (pl) (Wang et al., 2020). The mechanism action of streptokinase is presented in Figure 14.3.
Comparison of conventional and extractive fermentation using aqueous two-phase system to extract fibrinolytic proteases produced by Bacillus stearothermophilus DPUA 1729
Published in Preparative Biochemistry & Biotechnology, 2021
Raimundo Felipe da Cruz Filho, Januário Gama dos Santos, Rosana Antunes Palheta, Valéria Carvalho Santos-Ebinuma, Daniela de Araújo Viana Marques, Maria Francisca Simas Teixeira
Thrombolytic drugs such as tissue plasminogen activator (t-PA), urokinase plasminogen activator (u-PA) and streptokinase are used in the treatment of cardiovascular diseases. In emergencies cases, activase® (serine protease), which is an activator of tissue plasminogen (t-PA) produced by recombinant DNA technology, is also used. All of these drugs have effective action in a short time but they are still expensive,[5,6] presented undesirable side effects, which include excessive bleeding, anaphylaxis and recurrence at the site of the residual thrombosis and have immunogenic effects.[7,8] In this way, alternative drugs and treatments are of great interest. In this sense, fibrinolytic enzymes, also known as nattokinase, which can reduce fibrinogen levels and degrade fibrin branched.[6,9] have gained attention due to their low cost of production and commercialization (three-time cheaper than conventional drugs), besides reduced side effects.[7,10] Fibrinolytic enzymes show the ability to dissolve the fibrin in blood clots represented by the fibrinolytic activity.[11]