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m-钙激活酶的分离纯化方法研究 被引量:3

Study on the Purification of m-calpain
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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。 This experiment was conducted for further investigation into m-calpain activity and its role in beef aging. Fresh yellow cattle spleen (within 30min postmortem) was obtained and treated with proedures such as ultrahigh refrigeration homogenization, ionic exchange chromatography, hydrophobic chromatography, etc. The resulted m-calpain with specific activity 39.7U/mg was verified by way of SDS-PAGE.
出处 《食品科学》 EI CAS CSCD 北大核心 2006年第3期30-33,共4页 Food Science
基金 国家自然科学基金(303710176) 高等学校博士点基金(2002037006) 江苏省自然科学基金(BK2003078)
关键词 钙激活酶系统 m-钙激活酶 纯化 calpain system, m-calpain purification
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