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Highly potent fibrinolytic serine protease from Streptomyces

Paper ID Volume ID Publish Year Pages File Format Full-Text
17567 42680 2011 6 PDF Available
Title
Highly potent fibrinolytic serine protease from Streptomyces
Abstract

We introduce a highly potent fibrinolytic serine protease from Streptomyces omiyaensis (SOT), which belongs to the trypsin family. The fibrinolytic activity of SOT was examined using in vitro assays and was compared with those of known fibrinolytic enzymes such as plasmin, tissue-type plasminogen activator (t-PA), urokinase, and nattokinase. Compared to other enzymes, SOT showed remarkably higher hydrolytic activity toward mimic peptides of fibrin and plasminogen. The fibrinolytic activity of SOT is about 18-fold higher than that of plasmin, and is comparable to that of t-PA by fibrin plate assays. Furthermore, SOT had some plasminogen activator-like activity. Results show that SOT and nattokinase have very different fibrinolytic and fibrinogenolytic modes, engendering significant synergetic effects of SOT and nattokinase on fibrinolysis. These results suggest that SOT presents important possibilities for application in the therapy of thrombosis.

Keywords
SOT, Streptomyces omiyaensis serine protease; t-PA, tissue-type plasminogen activator; NK, nattokinase; FRETS, fluorescence energy transfer substrate; Km, kanamycinSerine protease; Fibrinolytic enzyme; Streptomyces; FRETS
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Highly potent fibrinolytic serine protease from Streptomyces
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 48, Issue 1, 5 January 2011, Pages 7–12
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us