Devaraja, S. and Nagaraju, S. and Mahadeswaraswamy, Y. H. and Girish, K. S. and Kemparaju, K. (2008) A low molecular weight serine protease: Purification and characterization from Hippasa agelenoides (funnel web) spider venom gland extract. Toxicon, 52 (1). 130 - 138. ISSN 1879-3150
Full text not available from this repository. (Request a copy)Abstract
Despite the long history Kaiser, E., 1956. Enzymatic activity of spider venoms. In: Buckley, E.E., Porges, N. (Eds.), Venoms. American Association for the Advancement of Science, Washington, DC, pp. 91–93 on proteolytic activity, no study so far claims the isolation of a serine protease from the spider venom/venom gland extract. Therefore, the present study describes the isolation and characterization of a low molecular weight serine protease from Hippasa agelenoides venom gland extract. The protease (Hag-protease) was purified to homogeneity using the combination of gel-permeation and ion-exchange chromatography. The molecular mass was found to be 16.350kDa by matrix-assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry. Hag-protease was optimally active at pH 7.5 and temperature of 37°C. PMSF abolished the enzyme activity while EDTA, EGTA, IAA, 1, 10-phenanthrolene did not. It hydrolyzed proteins such as casein, fibronectin and collagen type-I dose dependently but did not degrade gelatin and collagen type-IV. The isolated protease was non-lethal and devoid of hemorrhagic, myotoxic and edema forming activities. The light microscopy of Hag-protease treated skin tissue sections at the site of injection showed extensive damage of extracellular matrix (ECM) of hypodermis without causing any damage to blood vessels and capillaries. Similar damage of ECM of muscle tissue sections without affecting myocytes was noticed. Hag-protease was found to be procoagulant in property when studied plasma recalcification time.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Spider venom, , Hag-protease, Serine protease, Venom protease |
| Subjects: | C Chemical Science > Biochemistry |
| Divisions: | Department of > Biochemistry |
| Depositing User: | Manjula P Library Assistant |
| Date Deposited: | 20 Aug 2019 11:39 |
| Last Modified: | 20 Aug 2019 11:39 |
| URI: | http://eprints.uni-mysore.ac.in/id/eprint/6838 |
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