Study of alkaline phosphatase from human hydatidiform mole

Study was performed on purification of alkaline phosphatase from Hydatiform mole. The sample of mole Hydatidiform subjects from Taleghani Hospital, Tehran, Iran was studied. An Alkaline phosphatase from Human Hydatidiform mole was purified by a protocol involving solubilization using precipitation by butanol, acetone, Ammonium sulphate, Sephadex G[200], Ion exchange chromatography and preparative electrophoresis. The enzyme was purified 800-fold to apparent homogeneity. This enzyme has 5.2% carbohyrate content. The optimum Temperature and pH were 40 centigrade degree and 10.4, respectively. Human Hydatidiform mole alkaline phosphatase is a novel alkaline phosphatase

Study of the new human molehydatiform alkaline phosphatase

Alkaline Phosphatase [EC: 3.1.3.1] is synthesized by kidney, liver, bone, Intestine and placenta. This enzyme is a glycoprotein and dimmer 4 Zn+2 and Mn+2 in each dimmer. It hydrolyzes mono ester phosphate to organic compound and phosphate_in alkaline medium. The purpose of this research is to compare this enzyme with placental alkaline phosphatase. Human Molehydatiform was purified by folds of precipitation of bybutanol, acetone, Amoniumm sulphate, Sephadex G200, affinity chromatography and preparative electrophoresis. Human Molehydatiform was purified 611.8 times. We obtained specific activity, optimum temperature and optimum Ph equaling to 611.8 U/mg, 40 centigrade degrees and 10.4 respectively. Purified Human Molehydatiform Alkalie phosphatase is different from Human placental Alkaline phosphatase due to optimum pH and optimum temperature