Purification and characterization of a fibrinogenase from Vipera lebetina (desert adder) venom

A. Gasmi 1 M. Karoui 1 Z. Benlasfar 1 H. Karoui 1 M. El Ayeb 1 K. Dellagi 1
1 Institut Pasteur de Tunis
Abstract : A fibrinogenase from Vipera lebetina venom was isolated by gel filtration in a Superose 12 column prep grade HR 16/50 and by ion-exchange in a Mono Q HR 5/5 column. The purified enzyme, which was obtained with a yield of 8 mg from 60 mg of crude venom, is a glycoprotein having an isoelectric point of 5.9±0.1 and a mol. wt of 26,000±1000 as estimated by SDS-PAGE. The biochemical characterization of the enzyme revealed that it hydrolyzes readily the Bβ chain of fibrinogen and the Aα chain as well as fibrin and casein. Over a pH range from 4 to 11 the enzyme was not inactivated by a 20 min treatment at 90°C. The isolated fibrinogenase is inhibited by ethylenediamine tetraacetic acid, dithiothreitol and l-cysteine but not by phenylmethylsulfonyl fluoride. On the other hand, it is activated by Ca2+ and Mg2+. Purified fibrinogenase up to a dose of 100 μg/mouse shows no toxicity and has no hemorrhagic activity.
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Submitted on : Thursday, February 21, 2019 - 3:06:56 PM
Last modification on : Wednesday, June 12, 2019 - 11:03:08 AM

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A. Gasmi, M. Karoui, Z. Benlasfar, H. Karoui, M. El Ayeb, et al.. Purification and characterization of a fibrinogenase from Vipera lebetina (desert adder) venom. Toxicon, Elsevier, 1991, 29 (7), pp.827-836. ⟨10.1016/0041-0101(91)90219-H⟩. ⟨pasteur-02044503⟩

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