@article{ref1,
title="Purification and properties of hyaluronidase from Hippasa partita (funnel web spider) venom gland extract",
journal="Toxicon: Journal of the International Society on Toxinology",
year="2007",
author="Nagaraju, S. and Devaraja, Sannaningaiah and Kemparaju, K.",
volume="50",
number="3",
pages="383-393",
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 approximately 20-folds. The molecular mass was found to be 42.26 kDa by matrix-assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry. HPHyal was optimally active at pH 5.8 at 37 degrees C and in the presence of 300 mM 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.<p /><p>Language: en</p>",
language="en",
issn="0041-0101",
doi="10.1016/j.toxicon.2007.04.007",
url="http://dx.doi.org/10.1016/j.toxicon.2007.04.007"
}