食品科学 ›› 2006, Vol. 27 ›› Issue (3): 30-33.

• 基础研究 • 上一篇    下一篇

m-钙激活酶的分离纯化方法研究

 黄明, 徐幸莲, 马汉军, 赵莲, 周光宏   

  1. 南京农业大学农业部农畜产品加工与质量控制重点开放实验室
  • 出版日期:2006-03-15 发布日期:2011-09-06

Study on the Purification of m-calpain

 HUANG  Ming, XU  Xing-Lian, MA  Han-Jun, ZHAO  Lian, ZHOU  Guang-Hong   

  1. Key Laboratory of Agricultural and Animal Products Processing and Quality Control, Ministry of Agriculture,Nanjing Agricultural University, Nanjing 210095, China
  • Online:2006-03-15 Published:2011-09-06

摘要: 本试验对牛脾脏中的m-钙激活酶进行了分离纯化,以便进一步研究其动力学特性和在牛肉成熟中的作用。对宰后30min牛肉匀浆后利用超高速冷冻离心、离子交换层析、疏水层析等技术,从中分离纯化出了m-钙激活酶,测得其比活力为39.7U/mg。利用变性电泳对纯化后的样品进行了验证。

关键词: 钙激活酶系统, m-钙激活酶, 纯化

Abstract:  This experiment was conducted for further investigation into m-calpain activity and its role in beef aging. Fresh yellowcattle spleen (within 30min postmortem) was obtained and treated with procedures such as ultrahigh refrigeration homogenization,ionic exchange chromatography, hydrophobic chromatography, etc. The resulted m-calpain with specific activity 39.7U/mg wasverified by way of SDS-PAGE .

Key words:  , calpain system; m-calpain; purification;