کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1191971 | 963599 | 2006 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Characteristics of carboxypeptidase B from pyloric ceca of the starfish Asterina pectinifera
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
Carboxypeptidase B was purified from the pyloric ceca of the starfish, Asterina pectinifera. The final enzyme preparation was nearly homogeneous in sodium dodecyl sulfate–polyacrylamide gel electrophoresis and its molecular weight was estimated as approximately 34,000. The value of the specificity constant (kcat/Km) for hydrolysis of benzoyl-glycyl-l-arginine by the purified enzyme was 1.72 × 105 M−1 s−1. The optimal pH and the optimal temperature of the enzyme were pH 7.5 and 55 °C, respectively. The enzyme was unstable above 50 °C and below pH 5.0. The enzyme was activated by Co2+, and inhibited by EDTA. The N-terminal amino acid sequence of the enzyme was determined as ATFDYNKYHSYQEIMDWVTN.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 95, Issue 2, March 2006, Pages 264–269
Journal: Food Chemistry - Volume 95, Issue 2, March 2006, Pages 264–269
نویسندگان
Hideki Kishimura, Kenji Hayashi, Seiichi Ando,