Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2450814 | Meat Science | 2011 | 6 Pages |
Abstract
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).
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Authors
Jason Krause, Shonisani C. Tshidino, Tomohisa Ogawa, Yasuharu Watanabe, Vaughan Oosthuizen, Benesh Somai, Koji Muramoto, Ryno J. Naudé,