摘要
根据过氧化氢酶的催化特性,采用盐析,透析,离心等技术,从大鼠肝脏中分离纯化过氧化氢酶,提纯倍数达到26倍,酶活性回收率为57%。为一般实验室分离纯化大鼠过氧化氢酶提供了一种有效的方法。酶学性质研究表明,该酶最适温度为37℃,最适pH值为7.5,在此条件下,以过氧化氢为底物的Km值为56 mmol.L-1。
According to the properties of catalase, we have got catalase from rat liver through the techniques of salting out,dialysis and centrifugation. The purification index was 26 and the recovery was 57%. This provided an effective method for the purification of rat liver catalase. The optimum temperature and pH of the rat catalase in liver were 37℃ and 7.5. The Km of substrate H2O2 was 56mmol · L^-1 , based on the optimum temperature and pH.
出处
《氨基酸和生物资源》
CAS
2009年第2期56-58,61,共4页
Amino Acids & Biotic Resources
基金
河北省教育科学研究"十一五"规划重点课题(0602040308020341)
