کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2066030 | 1076957 | 2007 | 11 صفحه PDF | دانلود رایگان |

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 42.26 kDa by matrix-assisted laser desorption ionization time of flight (MALDI-TOF) mass spectrometry. HPHyal was optimally active at pH 5.8 at 37 °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.
Journal: Toxicon - Volume 50, Issue 3, 1 September 2007, Pages 383–393