کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2450814 | 1109662 | 2011 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and partial characterization of ostrich skeletal muscle cathepsin D and its activity during meat maturation
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش تغذیه
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چکیده انگلیسی
Cathepsin D was purified from ostrich (Struthio camelus) skeletal muscle using pepstatin-A chromatography. The enzyme was comprised of two subunits (29.1 and 14 kDa). The N-terminal amino acid sequence of both subunits were determined and showed high amino acid sequence identity to other cathepsin D homologs. Ostrich cathepsin D was optimally active at pH 4 and at a temperature of 45 °C, and was strongly inhibited by pepstatin-A (Ki = 3.07 × 10− 9 M) and dithiothreitol. Cathepsin D activities from five ostriches were monitored over a 30-day period. Cathepsin D remained substantially active throughout the 30-day storage period with an average remaining activity of 112 ± 8.57% at day 30 (mean value from 5 ostriches).
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Meat Science - Volume 87, Issue 3, March 2011, Pages 196–201
Journal: Meat Science - Volume 87, Issue 3, March 2011, Pages 196–201
نویسندگان
Jason Krause, Shonisani C. Tshidino, Tomohisa Ogawa, Yasuharu Watanabe, Vaughan Oosthuizen, Benesh Somai, Koji Muramoto, Ryno J. Naudé,