کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8327509 | 1540202 | 2018 | 31 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A novel fibrinolytic serine metalloprotease from the marine Serratia marcescens subsp. sakuensis: Purification and characterization
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
This study demonstrates the purification and characterization of a fibrinolytic serine metalloprotease from the marine Serratia marcescens subsp. sakuensis (KU296189.1). The purified enzyme (1033â¯U/mg) had a molecular weight of 43â¯KDa, with optimum pH and temperature being 7 and 55â¯Â°C. The in vitro half-life of the fibrinolytic enzyme at 37â¯Â°C was found to be 19â¯h. The kinetic constants, Km and Vmax of the purified enzyme determined using fibrin as substrate was 0.66â¯mg/mL and 158.73â¯U/mL. The Kcat and catalytic efficiency of the enzyme was found to be 12.21â¯minâ1 and 18.32â¯mL/(mgâ¯min) respectively. The fibrinolytic enzyme did not show any proteolytic activity towards blood plasma proteins like haemoglobin, γ-globulins and transferrin. In vitro studies revealed that the fibrinolytic enzyme displayed 38% clot lysis for a period of 3â¯h which was higher than that displayed by streptokinase and heparin. A total of seven peptide sequences were obtained after the LC-MS/MS-TOF analysis, out of which only four sequences showed 67% homology with the sequences of the other proteases. All these results suggest its novelty and potential application in thrombolytic therapy.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 112, June 2018, Pages 110-118
Journal: International Journal of Biological Macromolecules - Volume 112, June 2018, Pages 110-118
نویسندگان
Anusha Krishnamurthy, Prasanna Devarbhat Belur,