کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
4357767 1300104 2008 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Purification and characterization of fibrinolytic metalloprotease from Perenniporia fraxinea mycelia
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک علوم کشاورزی و بیولوژیک (عمومی)
پیش نمایش صفحه اول مقاله
Purification and characterization of fibrinolytic metalloprotease from Perenniporia fraxinea mycelia
چکیده انگلیسی

In this study we purified and characterized a fibrinolytic protease from the mycelia of Perenniporia fraxinea. The apparent molecular mass of the purified enzyme was estimated to be 42 kDa by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), fibrin zymography and size exclusion using fast protein liquid chromatography (FPLC). The first 20 amino acid residues of the N-terminal sequence were ASYRVLPITKELLPPEFFVA, which shows a high degree of similarity with a fungalysin metallopeptidase from Coprinopsis cinerea. The optimal reaction pH value and temperature were pH 6.0 and 35–40 °C, respectively. Results for the fibrinolysis pattern showed that the protease rapidly hydrolyzed the fibrin α-chain followed by the β-chain. The γ–γ chains were also hydrolyzed, but more slowly. The purified protease effectively hydrolyzed fibrinogen, preferentially digesting the Aα-chains of fibrinogen, followed by Bβ- and γ-chains. We found that protease activity was inhibited by Cu2+, Fe3+, and Zn2+, but enhanced by the additions of Mn2+, Mg2+ and Ca2+ metal ions. Furthermore, the protease activity was inhibited by EDTA, and it was found to exhibit a higher specificity for the chromogenic substrate S-2586 for chymotrypsin, indicating that the enzyme is a chymotrypsin-like metalloprotease. The mycelia of P. fraxinea may thus represent a source of new therapeutic agents to treat thrombosis.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Mycological Research - Volume 112, Issue 8, August 2008, Pages 990–998
نویسندگان
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