Devaraja, S. and Girish, K. S. and Gowtham, Y. N. J. and Kemparaju, K. (2011) The Hag-protease-II is a fibrin(ogen)ase from hippasa agelenoides spider venom gland extract: Purification, characterization and its role in hemostasis. TOXICON, 57 (2). pp. 248-258.
Full text not available from this repository. (Request a copy)Abstract
The current study describes the biochemical, biophysical and pharmacological properties of Hag-protease-II from Hippasa agelenoides spider venom gland extract. The Hag-protease-II was purified to homogeneity using gel filtration and ion-exchange chromatography. The molecular mass was found to be 28.749 kDa by MALDI-TOF mass spectrometry. PMSF abolished the activity while EDTA, EGTA, IAA and 1, 10-phenanthrolene did not. Hag-protease-II hydrolyzed casein, fibrinogen and fibrin, however it did not hydrolyze gelatin, fibronectin and collagen types-I and IV. It was non-lethal and devoid of hemorrhagic, myotoxic and edema forming activities. It dose dependently reduced re-calcification time of citrated human plasma. Strikingly; the Hag-protease-II coagulated the factor X deficient congenital human plasma. It hydrolyzed B beta-chain but, did not degrade A alpha- and gamma-chains of fibrinogen while, it hydrolyzed alpha-polymer and alpha-chain but not the beta-chain and gamma-gamma dimers of partially crosslinked fibrin clot. The Hag-protease-II induced aggregation of human platelets in PRP dose dependently, however it did not interfere in collagen induced aggregation of PRP and washed human platelets. (c) 2010 Elsevier Ltd. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Hippasa agelenoides; Spider venom; Hag-protease-II; serine protease; Fibrino(geno)lytic enzyme; Platelet aggregation |
| Subjects: | C Chemical Science > Chemistry |
| Divisions: | Department of > Chemistry |
| Depositing User: | Users 23 not found. |
| Date Deposited: | 18 Jun 2019 11:53 |
| Last Modified: | 18 Jun 2019 11:53 |
| URI: | http://eprints.uni-mysore.ac.in/id/eprint/2570 |
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