کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2064380 1544121 2016 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Expression and partial biochemical characterization of a recombinant serine protease from Bothrops pauloensis snake venom
ترجمه فارسی عنوان
بیان و خصوصی سازی بیوشیمیایی نسبی پروتئاز سرین نوترکیب از زهر مارماهی
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیوشیمی، ژنتیک و زیست شناسی مولکولی (عمومی)
چکیده انگلیسی


• rBpSP-II showed sequence identity ranging from 83% to 96% to other snake venom serine proteases.
• rBpSP-II showed activity on chromogenic substrates demonstrated thrombin-like activity.
• rBpSP-II can serve as template for synthesis of therapeutic agents to treat hemostatic disorders.

Snake venom serine proteases (SVSPs) are enzymes capable of interfering at several points of hemostasis. Some serine proteases present thrombin-like activity, which makes them targets for the development of therapeutics agents in the treatment of many hemostatic disorders. In this study, a recombinant thrombin-like serine protease, denominated rBpSP-II, was obtained from cDNA of the Bothrops pauloensis venom gland and was characterized enzymatically and biochemically. The enzyme rBpSP-II showed clotting activity on bovine plasma and proteolytic activity on fibrinogen, cleaving exclusively the Aα chain. The evaluation of rBpSP-II activity on chromogenic substrates demonstrated thrombin-like activity of the enzyme due to its capacity to hydrolyze the thrombin substrate. These characteristics make rBpSP-II an attractive molecule for additional studies. Further research is needed to verify whether rBpSP-II can serve as a template for the synthesis of therapeutic agents to treat hemostatic disorders.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Toxicon - Volume 115, 1 June 2016, Pages 49–54
نویسندگان
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