@article{0d4c59dc795c448f9209e37077f43fde,
title = "Purification and partial characterization of ostrich skeletal muscle cathepsin D and its activity during meat maturation",
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 14kDa). 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=3.07×10-9M) 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).",
keywords = "Cathepsin D, Ostrich muscle, Pepstatin-A, Postmortem proteolysis",
author = "Jason Krause and Tshidino, {Shonisani C.} and Tomohisa Ogawa and Yasuharu Watanabe and Vaughan Oosthuizen and Benesh Somai and Koji Muramoto and Naud{\'e}, {Ryno J.}",
note = "Funding Information: The authors gratefully acknowledge the financial support from the National Research Foundation (South Africa) and the Japanese Society for the Promotion of Science (Japan) and express their sincere gratitude to the Grahamstown ostrich abattoir (South Africa), for their generous supply of ostrich skeletal muscle.",
year = "2011",
month = mar,
doi = "10.1016/j.meatsci.2010.10.009",
language = "English",
volume = "87",
pages = "196--201",
journal = "Meat Science",
issn = "0309-1740",
publisher = "Elsevier BV",
number = "3",
}