Purification and properties of hyaluronidase from Hippasa partita (funnel web spider) venom gland extract

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

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Official URL: https://doi.org/10.1016/j.toxicon.2007.04.007


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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