Venkatesh Kumar, R. and Yariswamy, M. and Joshi, V. and Dharmappa, K. K. and Venkatesha, S. H. and Sharath, B. K. and Vishwanath, B. S. (2013) Malabarase, a serine protease with anticoagulant activity from Trimeresurus malabaricus venom. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 164 (2). pp. 111-116. ISSN 1096-4959
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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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | animal experiment, Animals, Anticoagulants, anticoagulation, article, blood clotting, blood clotting time, Blood Coagulation, Chromatography, controlled study, Creatine Kinase, Crotalid Venoms, Electrophoresis, Fibrinogen, gel permeation chromatography, Hemorrhage, High Pressure Liquid, Humans, Ion Exchange, ion exchange chromatography, malabarase, malabarin, male, Mass, matrix assisted laser desorption ionization time of flight mass spectrometry, Matrix-Assisted Laser Desorption-Ionization, metalloproteinase, Mice, molecular weight, Molecular Weight, mouse, nonhuman, Polyacrylamide Gel, polyacrylamide gel electrophoresis, priority journal, protein hydrolysis, Reverse-Phase, reversed phase high performance liquid chromatography, sephadex, Serine Proteases, serine proteinase, Skin, snake, snake venom, Spectrometry, Time Factors, trimarin, Trimeresurus, Trimeresurus malabaricus, Trimeresurus malabaricus venom, unclassified drug, Whole Blood Coagulation Time |
| Subjects: | C Chemical Science > Biochemistry |
| Divisions: | Department of > Biochemistry PG Centre Hassan > Bioscience |
| Depositing User: | Arshiya Kousar Library Assistant |
| Date Deposited: | 15 Oct 2019 05:31 |
| Last Modified: | 15 Oct 2019 05:32 |
| URI: | http://eprints.uni-mysore.ac.in/id/eprint/8979 |
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