Nagaraju, S. and Devaraja, S. and Kemparaju, K. (2007) Purification and properties of hyaluronidase from Hippasa partita (funnel web spider) venom gland extract. Toxicon, 50 (3). 383 - 393. ISSN 0041-0101
Full text not available from this repository. (Request a copy)Abstract
Spider venom is a complex mixture of protein and peptide toxins. Hyaluronidase a ‘spreading factor’ has not been studied extensively in spider venom. In this paper, we describe the purification and characterization of a hyaluronidase from Hippasa partita venom gland extract. Hyaluronidase (HPHyal) has been purified by the successive chromatography on a Sephadex G-100 and on CM-Sephadex C-25 columns. HPHyal has been purified to an extent of about ∼20-folds. The molecular mass was found to be 42.26kDa by matrix-assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry. HPHyal was optimally active at pH 5.8 at 37°C and in the presence of 300mM NaCl in the reaction mixture. HPHyal showed absolute specificity for hyaluronan and belongs to neutral active group of enzymes. HPHyal revealed single-precipitin line, while venom gland extract revealed multiple bands in Western blotting with the antiserum prepared against venom gland extract. HPHyal indirectly potentiates the myotoxicity of VRV-PL-VIII myotoxin and also the hemorrhagic potency of hemorrhagic complex-I. Cations, Na+ and K+ enhanced the activity and chloride ions do not have any effect while, divalent cations, inhibited the enzyme activity.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Hyaluronidase, Spreading factor, Hyaluronic acid, venom gland extract. |
| Subjects: | C Chemical Science > Biochemistry |
| Divisions: | Department of > Biochemistry |
| Depositing User: | C Swapna Library Assistant |
| Date Deposited: | 25 Sep 2019 05:43 |
| Last Modified: | 25 Sep 2019 05:43 |
| URI: | http://eprints.uni-mysore.ac.in/id/eprint/8495 |
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