کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1952720 1057224 2010 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Enzymatic and structural characterization of a basic phospholipase A2 from the sea anemone Condylactis gigantea
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Enzymatic and structural characterization of a basic phospholipase A2 from the sea anemone Condylactis gigantea
چکیده انگلیسی

This work aimed at the isolation and structural/functional characterization of a phospholipase A2 (CgPLA2) from the extract of the anemone Condylactis gigantea. CgPLA2 was isolated with a high purity level through three chromatographic steps, showing pI ˜ 8.6 and molecular weights of 14,500 and 29,000 for the monomer and dimer, respectively. CgPLA2 showed a high catalytic activity upon fluorescent phospholipids inducing no direct hemolytic activity. This enzyme, which is Ca2+-dependent, showed a lower stability against temperature and pH variations when compared with snake venom enzymes. The enzymatic activity was significantly reduced or completely abolished after chemical modification of CgPLA2 with BPB. Its cDNA was then obtained, with 357 base pairs which codified for a mature protein of 119 amino acid residues. A comparative analysis of the primary structure of CgPLA2 revealed 84%, 61%, 43% and 42% similarity to the PLA2s from Adamsia carciniopados, Nematostella vectensis, Vipera russelli russelli and Bothrops jararacussu, respectively.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimie - Volume 92, Issue 8, August 2010, Pages 1063–1071
نویسندگان
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