摘要
组织蛋白酶L很难通过常规的肌动球蛋白提取方法完全去除.由琼脂糖凝胶6B凝胶层析图谱显示,组织蛋白酶L的活性主峰明显偏离肌动球蛋白主峰,表明该酶是肌动球蛋白非结合型酶.凝胶柱层析后测定L型组织蛋白酶粗酶液(Lmix)的活性,结果表明Lmix的热稳定性与pH和温度密切相关,其最适pH为5.0,最适温度为45℃.在最适pH5.0时,Lmix的活性随NaCl浓度的增加而增大.专一性底物及酶激活剂、抑制剂影响研究表明,Lmix为内含巯基的半胱氨酸型组织蛋白酶.
Cathepsin L could not be removed completely during conventional actomyosin extraction and still remained in the actomyosin of red bulleye surimi.Sepharose 6B gel filtration profile showed that the main peak of cathepsin L was separated from that of actomyosin suggesting the enzyme was non-binding to actomyosin.Optimal pH of cathepsin L in actomyosin and Lmix was 5.0 and the optimal temperature of Lmix was 45℃.Stability of Lmix was closely related to temperature and pH.At optimal pH5.0,activity of Lmix increased with the increase of NaCl concentration.Studies of substrate specificity and effects of activators and inhibitors confirmed Lmix to be a thiol-type cysteine protease.
出处
《合肥学院学报（自然科学版）》
2010年第3期66-71,共6页
Journal of Hefei University :Natural Sciences
基金
国家自然科学基金项目(NSFC30972282)
中央高校基本科研业务费专项资金(009QNA6020)资助
