Evaluation of the Fi-fibrinolytic Potential of Recombinant Subtilisin from Bacillus subtilis
Yazarlar (3)
Doç. Dr. Canan GÜLMEZ SAMSA Iğdır Üniversitesi, Türkiye
Prof. Dr. Onur ATAKİŞİ Kafkas Üniversitesi, Türkiye
Melek Öztürkler
| Makale Türü | Özgün Makale (Diğer hakemli uluslarası dergilerde yayınlanan tam makale) | ||
| Dergi Adı | JSMC Biochem Mol Res | ||
| Dergi ISSN | 2638-4698 | ||
| Dergi Tarandığı Indeksler | Google Scholar | ||
| Makale Dili | İngilizce | Basım Tarihi | 04-2019 |
| Cilt / Sayı / Sayfa | 1 / 1 / 3–5 | DOI | – |
| UAK Araştırma Alanları |
Veteriner Biyokimyası
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| Özet |
| The aim of this study was to investigate the potential for the treatment of thromboembolic diseases by determining the fibrinolytic, fibrinogenolytic activities and substrate specificity of the recombinant subtilisin from Bacillus subtilis strain PTTC 1023. The subtilisin gene from Bacillus sp. was synthesized, cloned into the vector pD441-NH and expressed in E. coli BL21 (DE3). Recombinant subtilisin (~ 40 kDa) was purified in a single-step procedure by affinity chromatography. The fibrinolytic, fibrinogenolytic activities and substrate specificity of the pure recombinant enzyme was determined. The recombinant protease of B. subtilis displayed an optimum fibrinolytic activity at pH 7.5 and 37 C. The α, β and ϒ-ϒ chains of fibrinogen were totally degraded by the recombinant enzymes at 37 C for 30 min. However, the ϒ chains were more resistant to enzyme digestion in all times. The clear zones produced by recombinant enzyme and plasmin on the fibrin plate did not significant difference The enzyme showed the highest proteolytic activity against fibrin, while it showed low activity against serum albumin and lactoferrin. The enzyme did not show activity against immunoglobulin. The data obtained indicates that recombinant enzyme is a plasmin-like fibrinolytic serine protease. The recombinant protease may have potential applications in the prevention and treatment of thrombosis and other cardiovascular diseases. |
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