Alkaline phosphatase (AP, E.C. 3.1.3.1) was partially purified from goat kidney by ammonium sulphate precipitation, DEAE-trisacryl and gel chromatographic methods. The specific activity of the purified enzyme was 0.1 units/ mg protein. The activity of the enzyme was linear upto 25 mmutes with 0.002 units of enzyme. The optimum temperature and pH for enzyme activity were 40 "C and 11.0 respectively. The enzyme was resistant to heat up to 50 IIC while its activity was irreversibly destroyed at 60 "C. L-Phenylalanine, zinc chloride, 2-mercaptoethanol, EDT A, and pyridoxal phosphate inhibited enzyme activity and there was no effect of L-Ieucine and L-tryptophan. Keeping in view these properties, the purified enzyme from goat kidney resembled intestinal alkaline phosphatase.
MUHAMMAD ZABTA ,MUHAMMAD ASHRAF ,ASMA SAEED ,TANVEER SHARIF ,
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