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°C, 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.