Purification and Some Properties of Alkaline Phosphatase from the Liver of Bos taurus

摘要：

Alkaline phosphatase was isolated and purified from the cattle (Bos taurus) liver by means of homogeni-zeation, n-butanol disposal, thermal denaturation, ultrafilt-ration, DEAE-Sepharose column chromatography and Sephacryl S-200 gel filtration chromatography. Its specific activity was 19863.50, and the purification fold was 228.74. Its optimum pH and temperature was 10.0 and 45℃, respectively. Na+, K+and Li+had no effect on the activity of the enzyme. Mg2+activated the enzyme while Zn2+, Cu2+inhibited its activity. The Km was 0.64mmol/L.

作者: TANG Liang-ting FU Wei-li WANG Song ZHU Hong TANG Yun-ming

作者单位: Key Laboratory of Eco-environments in Three Gorges Reservoir Region Ministry of Education, Chongqing Sweetpotato Engineering Research Center, School of Life Science, Southwest University,Chongqing 400715, China

会议类型: 国际会议

会议名称: The 4th International Conference on Bioinformatics and Biomedical Engineering(第四届IEEE生物信息与生物医学工程国际会议 iCBBE 2010)

会议地点: 成都

会议语种:英文

页码: 1-4

在线出版日期: 2010-06-18（万方平台首次上网日期，不代表论文的发表时间）