Malabarase, a serine protease with anticoagulant activity from Trimeresurus malabaricus venom
| Autor: | K. K. Dharmappa, Raju Venkatesh Kumar, B.K. Sharath, M. Yariswamy, Vikram Joshi, Shivaprasad H. Venkatesha, Bannikuppe S. Vishwanath |
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| Rok vydání: | 2013 |
| Předmět: |
Time Factors
Whole Blood Coagulation Time Physiology Trimeresurus Hemorrhage Venom Fibrinogen Biochemistry Mice Crotalid Venoms medicine Animals Humans Blood Coagulation Creatine Kinase Molecular Biology Chromatography High Pressure Liquid Skin Serine protease Chromatography Reverse-Phase biology Molecular mass Anticoagulants Chromatography Ion Exchange biology.organism_classification Molecular biology Molecular Weight Coagulation Clotting time Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein Electrophoresis Polyacrylamide Gel Serine Proteases Trimeresurus malabaricus medicine.drug |
| Zdroj: | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 164:111-116 |
| ISSN: | 1096-4959 |
| DOI: | 10.1016/j.cbpb.2012.11.004 |
| Popis: | In the present study we describe the purification and characterization of Malabarase, a serine protease from Trimeresurus malabaricus venom. Purification was achieved by gel-permeation chromatography on Sephadex G-75 followed by ion-exchange chromatography on CM Sephadex C-25. Homogeneity of Malabarase was confirmed by RP-HPLC. Malabarase is a monomer that migrated as a single protein band on SDS-PAGE under both reducing and non-reducing conditions. The molecular mass of Malabarase was determined to be 23.4 kDa using MALDI-TOF mass spectrometry. Malabarase is the first serine protease purified from T. malabaricus venom and is selective for fibrinogen. Malabarase hydrolyzes Aα and Bβ but not γ-chains of fibrinogen similar to the metalloproteases, Malabarin and Trimarin, isolated from the same venom. However, the action of Malabarase on plasma coagulation is opposite than those of Malabarin, Trimarin and the whole venom. Malabarase significantly prolonged plasma coagulation time from 152-341 s; whereas Malabarin, Trimarin, and whole venom, greatly reduce plasma clotting time from 152 to 12, 48, and 14 s, respectively. Malabarase did not show hemorrhagic or myotoxic activity. In contrast, Malabarin, Trimarin and whole venom are highly hemorrhagic and myotoxic. These observations support the specificity of Malabarase towards fibrinogen and its non-toxic nature. In conclusion, Malabarase is a fibrinogen-specific, anti-coagulant, and non-toxic serine protease. Its selective action and non-toxic nature might make it useful for treating thrombotic disorders. |
| Databáze: | OpenAIRE |
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