کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2066030 1076957 2007 11 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Purification and properties of hyaluronidase from Hippasa partita (funnel web spider) venom gland extract
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیوشیمی، ژنتیک و زیست شناسی مولکولی (عمومی)
پیش نمایش صفحه اول مقاله
Purification and properties of hyaluronidase from Hippasa partita (funnel web spider) venom gland extract
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Toxicon - Volume 50, Issue 3, 1 September 2007, Pages 383–393
نویسندگان
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