鸵鸟骨骼肌组织组织蛋白酶 D 的纯化及其部分特性分析和宰后成熟过程中的活性变化。

Purification and partial characterization of ostrich skeletal muscle cathepsin D and its activity during meat maturation.

机构信息

Department of Biochemistry and Microbiology, Nelson Mandela Metropolitan University, P.O. Box 7700, Port Elizabeth 6000, South Africa.

出版信息

Meat Sci. 2011 Mar;87(3):196-201. doi: 10.1016/j.meatsci.2010.10.009. Epub 2010 Oct 16.

DOI:10.1016/j.meatsci.2010.10.009

PMID:21055883

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 (K(i)=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).

摘要

组织蛋白酶 D 从鸵鸟（Struthio camelus）骨骼肌中使用胃蛋白酶抑制剂 A 层析法纯化。该酶由两个亚基（29.1 和 14 kDa）组成。两个亚基的 N-末端氨基酸序列被确定，并显示出与其他组织蛋白酶 D 同源物的高氨基酸序列同一性。鸵鸟组织蛋白酶 D 在 pH 4 和 45°C 的温度下具有最佳活性，并且被胃蛋白酶抑制剂 A（K(i)=3.07×10(-9)M）和二硫苏糖醇强烈抑制。在 30 天的时间内监测了五只鸵鸟的组织蛋白酶 D 活性。组织蛋白酶 D 在 30 天的储存期内保持了相当高的活性，在第 30 天的平均剩余活性为 112±8.57%（来自 5 只鸵鸟的平均值）。