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牛心细胞色素C氧化酶的纯化

The purification of cytochrome C oxidase from bovine heart
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摘要 本文应用硫酸铵分级沉淀、Phenyl-Sepharose CL-4B 疏水层析和 Cytocrome C-Sepharose 4B亲和层析的方法,从牛心肌中分离纯化了细胞色素C氧化酶。产品Heme a含量为16.32nmol/mg Pr,铜原子含量为15.24n atoms/ms Pr。活性实验表明,去脂的细胞色素 C氧化酶活性下降,加入Tween 80可使活性明显提高,说明疏水环境对酶的催化功能有保护作用。 This paper reports the purification of CCO from bovine heart with ammonium sulfate precipitation, phneyl - Sepharose CL-4B hydrophobic chromatographic and cytochrome C-Sepharose 4B affinity chromatographic methods. The content of heme a and copper in the purified CCO reached 16. 3 n mols/mgPr and 15. 24 n atoms/mgPr. It was indicated that the activity of CCO decreased after removing the lipids. and rised by adding Tween 80. Hydrophobic environment of CCO activity site provided the protection to the catalytic function.
出处 《白求恩医科大学学报》 CSCD 1993年第5期505-506,共2页 Journal of Norman Bethune University of Medical Science
关键词 细胞色素 氧化酶 分离 提纯 酶激活 cytochrome oxidases/IP: chromatography affinity/MT: enzyme activation
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