کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9602696 | 42736 | 2005 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and characterization of a novel proteinase A inhibitor from Ganoderma lucidum by submerged fermentation
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
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چکیده انگلیسی
A novel proteinase A inhibitor was purified from Ganoderma lucidum. The purification was carried out by ethanol precipitation (50-80%), ACA44 gel filtration and Source 30Q anion exchange, respectively. The molecular mass of the inhibitor was 38 kDa as estimated via SDS-PAGE and gel filtration. Its carbohydrate content was up to 70%. β-Elimination revealed that the linkage between the glycan and the core protein backbone might be O-linkage. This inhibitor showed a remarkable heat stability. By investigating the interaction between this inhibitor and a variety of proteinases, it is indicated that the inhibitor was more specific against yeast proteinase A than other proteinases. The dissociation constants (Ki) and concentration required for 50% inhibition (IC50) for proteinase A were 2.7 Ã 10â6 M and 0.16 mg/ml, respectively.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Enzyme and Microbial Technology - Volume 36, Issues 2â3, 1 February 2005, Pages 357-361
Journal: Enzyme and Microbial Technology - Volume 36, Issues 2â3, 1 February 2005, Pages 357-361
نویسندگان
Ya-Ping Tian, Ke-Chang Zhang,