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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Sun, Zhibin Liu, Pingping Cheng, Guangyan Zhang, Biying Dong, Weiliang Su, Xingli Huang, Yan Cui, Zhongli Kong, Yi |
| Description | Author Affiliation: Sun Z ( Key Laboratory of Environmental Microbiology of Ministry of Agriculture, Nanjing Agricultural University, Nanjing 210095, People's Republic of China.); Liu P ( Key Laboratory of Environmental Microbiology of Ministry of Agriculture, Nanjing Agricultural University, Nanjing 210095, People's Republic of China.); Cheng G ( College of Life Sciences and Technology, China Pharmaceutical University, Nanjing 210009, People's Republic of China.); Zhang B ( Key Laboratory of Environmental Microbiology of Ministry of Agriculture, Nanjing Agricultural University, Nanjing 210095, People's Republic of China.); Dong W ( Key Laboratory of Environmental Microbiology of Ministry of Agriculture, Nanjing Agricultural University, Nanjing 210095, People's Republic of China.); Su X ( College of Life Sciences and Technology, China Pharmaceutical University, Nanjing 210009, People's Republic of China.); Huang Y ( Key Laboratory of Environmental Microbiology of Ministry of Agriculture, Nanjing Agricultural University, Nanjing 210095, People's Republic of China.); Cui Z ( Key Laboratory of Environmental Microbiology of Ministry of Agriculture, Nanjing Agricultural University, Nanjing 210095, People's Republic of China. Electronic address: czl@njau.edu.cn.); Kong Y ( College of Life Sciences and Technology, China Pharmaceutical University, Nanjing 210009, People's Republic of China. Electronic address: yikong668@163.com.) |
| Abstract | Fibrinolytic proteases have potential applications in cardiovascular disease therapy. A novel fibrinolytic protease, AfeE, with strong thrombolytic activity was purified from Streptomyces sp. CC5. AfeE displayed maximum activity at 40°C in the pH range of 7.0-12.0. It was strongly inhibited by serine protease inhibitor phenylmethanesulfonylfluoride, soybean trypsin inhibitor, tosyl-l-lysine chloromethyl ketone and tosyl-l-phenylalanine chloromethyl ketone. The activity of the enzyme was partially inhibited by Cu(2+), Co(2+) and Zn(2+). AfeE exhibited higher substrate specificity for fibrin than fibrinogen, which has rarely been reported in fibrinolytic enzymes. AfeE also showed high thrombolytic activity in a carrageenan-induced mouse tail thrombosis model. AfeE prolonged prothrombin time, activated partial thromboplastin time, and thrombin time in rat blood. A bleeding time assay revealed that AfeE did not prolong bleeding time in mice at a dose of 1mg/kg. No acute cytotoxicity was observed for AfeE at 320µg/well in human umbilical vein endothelial cells. The afeE gene was cloned from the genome of Streptomyces sp. CC5. Full-length AFE-CC5E contained 434 amino acids and was processed into a mature form consisting 284 amino acids by posttranslational modification, as revealed by high-resolution mass spectrometry analysis. These results indicate that AfeE is a prospective candidate for antithrombotic drug development. |
| File Format | HTM / HTML |
| ISSN | 01418130 |
| Volume Number | 85 |
| e-ISSN | 18790003 |
| Journal | International Journal of Biological Macromolecules |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-04-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Biochemistry Endopeptidases Chemistry Pharmacology Fibrinolytic Agents Animals Blood Coagulation Drug Effects Disease Models, Animal Isolation & Purification Enzyme Activation Enzyme Stability Hydrogen-ion Concentration Ions Male Metals Mice Molecular Weight Streptomyces Enzymology Substrate Specificity Temperature Thrombosis Blood Drug Therapy Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Structural Biology Molecular Biology Biochemistry |
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