کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10880270 | 1076951 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and characterization of a hemorrhagic metalloproteinase from Bothrops lanceolatus (Fer-de-lance) snake venom
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کلمات کلیدی
PVDFPMSFSDSTEMEDSVMPN,N,N′,N′-tetramethylethylenediamine - N، N، N '، N'-tetramethylethylenediamineEDTA - اتیلن دی آمین تترا استیک اسید Ethylenediaminetetraacetic acid - اتیلینیدامین تتراستیک اسیدTame - تامHemorrhage - خونریزیpolyvinylidene difluoride - دی فلوئورید پلی وینیلیدینSnake venom - زهر مارsodium dodecyl sulphate - سدیم دودسیل سولفاتphenylmethylsulphonyl fluoride - فنیل متیل سولفونیل فلورایدMetalloproteinase - متالوپروتئیناز Snake venom metalloproteinase - متالوپروتئیناز زهر مارBothrops lanceolatus - هر دو لانسولاتوسProteolytic - پروتئولیتیک
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوشیمی، ژنتیک و زیست شناسی مولکولی (عمومی)
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Purification and characterization of a hemorrhagic metalloproteinase from Bothrops lanceolatus (Fer-de-lance) snake venom Purification and characterization of a hemorrhagic metalloproteinase from Bothrops lanceolatus (Fer-de-lance) snake venom](/preview/png/10880270.png)
چکیده انگلیسی
Bothrops snake venoms contain metalloproteinases that contribute to the local effects seen after envenoming. In this work, a hemorrhagic metalloproteinase (BlaH1) was purified from the venom of the snake Bothrops lanceolatus by a combination of gel filtration, affinity (metal chelating) and hydrophobic interaction chromatographies. The hemorrhagin was homogeneous by SDS-PAGE and had a molecular mass of 28 kDa that was unaltered by treatment with β-mercaptoethanol. BlaH1 gave a single band in immunoelectrophoresis and immunoblotting using commercial bothropic antivenom. BlaH1 had hemorrhagic, caseinolytic, fibrinogenolytic, collagenolytic and elastinolytic activities, but no phospholipase A2 activity. The hemorrhagic and caseinolytic activities were inhibited by EDTA, indicating that they were metal ion-dependent. In contrast, aprotinin, benzamidine and PMSF did not affect these activities. The caseinolytic activity of BlaH1 had a pH optimum of 8.0 and was stable in solution at up to 40 °C; activity was completely lost at â¥70 °C. The hemorrhagic activity was neutralized by commercial bothropic antivenom. These properties suggest that this new hemorrhagin belongs to class P-I snake venom metalloproteinases.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Toxicon - Volume 45, Issue 4, 15 March 2005, Pages 411-420
Journal: Toxicon - Volume 45, Issue 4, 15 March 2005, Pages 411-420
نویسندگان
Alessandra Stroka, José L. Donato, Cassian Bon, Stephen Hyslop, Albetiza Lôbo de Araújo,