کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2065970 1076952 2006 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Expression, purification and molecular modeling of recombinant fibrinogenase [IV], a metalloproteinase from Deinakistrodon acutus venom
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیوشیمی، ژنتیک و زیست شناسی مولکولی (عمومی)
پیش نمایش صفحه اول مقاله
Expression, purification and molecular modeling of recombinant fibrinogenase [IV], a metalloproteinase from Deinakistrodon acutus venom
چکیده انگلیسی

A novel metalloproteinase, recombinant fibrinogenase IV (rFIVa), was expressed and purified from Deinakistrodon acutus venom. It was a single chain protein with an apparent molecular weight 27 kDa and an isoeletric point of pH 7.1. RFIVa cleaved preferentially the Aα-chain and also cleaved Bβ, γ-chains of fibrinogen when the incubation time was prolonged. The proteolytic activity was inhibited by EDTA, l-cysteine, and DTT, indicating rFIVa was a metalloproteinase requiring disulfide bonds for its activity. It kept above 85% of the initial activity from pH 4.5–11, showed an equal maximum activity at the temperature range from 30 to 50 °C, and was inactivated by Zn2+, Cu2+ and Cd2+. Homology modeling of rFIVa showed that two highly conserved disulfide bonds (Cys159–Cys164 and Cys117–Cys197) was maintained from its structure, and it exhibited the characteristic conserved motif H142E143XXH146XXGXXH152, whose three histidine residues were involved in binding of the catalytically essential zinc ion. This work demonstrates the expression, purification and characterization of recombinant fibrinogenase IV, which belongs to class P-I metalloproteinase from D. acutus venom.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Toxicon - Volume 47, Issue 2, February 2006, Pages 241–248
نویسندگان
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