کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10880180 | 1076936 | 2005 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Properties and cDNA cloning of an antihemorrhagic factor (HSF) purified from the serum of Trimeresurus flavoviridis
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کلمات کلیدی
UTRFTCSnake serumNBShsfAntihemorrhagicTNBSN-bromosuccinimideSVMP2,4,6-Trinitrobenzene sulfonic acid - 2،4،6-ترینیتروبنسل سولفونیک اسیدPLI - بیشترcircular dichroism - رنگ تابی دورانیSnake venom - زهر مارMatrix-assisted laser desorption ionization time-of-flight mass spectrometry - طیف سنجی جرمی یونیزاسیون یونیزاسیون لیزر جذب ماتریسMALDI-TOF MS - مالدی توف MSMetalloproteinase - متالوپروتئیناز Snake venom metalloproteinase - متالوپروتئیناز زهر مارuntranslated region - منطقه غیر ترجمهPhospholipase A2 inhibitor - مهار کننده فسفولیپاز A2
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوشیمی، ژنتیک و زیست شناسی مولکولی (عمومی)
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چکیده انگلیسی
Habu serum factor (HSF) is a metalloproteinase inhibitor that is isolated from the serum of habu snake (Trimeresurus flavoviridis), and it can suppress snake venom-induced hemorrhage. In the present study, the inhibitory property and fundamental structure of HSF were analyzed in detail. HSF inhibited all the hemorrhagic and most of the non-hemorrhagic metalloproteinases tested from the venoms of T. flavoviridis and Gloydius halys brevicaudus. HSF was extremely stable in a broad range of temperature and pH, and the treatments with a temperature of 100 °C or pH ranging from 1 to 13 barely affects its reactivity against G. halys brevicaudus H6 protease. Gel filtration chromatography revealed that HSF binds to the H6 protease with a 1:1 molar ratio. A secondary structure profile of HSF that was monitored by circular dichroism spectrum remained unvaried up to 2 M urea. The activity of HSF was stoichiometrically abolished by chemical modification with 2,4,6-trinitrobenzene sulfonic acid and N-bromosuccinimide; this indicates that Lys and Trp residues in its sequence play a role in the inhibitory mechanism. In this study, the amino acid sequence of HSF that was obtained by cDNA cloning was identical to that reported previously, except for five substitutions. We concluded that these discrepancies reflect a difference in the places of capture of the snake specimens.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Toxicon - Volume 46, Issue 8, 15 December 2005, Pages 937-945
Journal: Toxicon - Volume 46, Issue 8, 15 December 2005, Pages 937-945
نویسندگان
Masanobu Deshimaru, Chie Tanaka, Kazuya Fujino, Narumi Aoki, Shigeyuki Terada, Shosaku Hattori, Motonori Ohno,