Study of alkaline phosphatase from human hydatidiform mole

Aberomand M., RAHIM F., Hosseini S. A.

Pakistan Journal of Medical Sciences, vol.24, no.3, pp.471-474, 2008 (Scopus) identifier identifier

  • Publication Type: Article / Article
  • Volume: 24 Issue: 3
  • Publication Date: 2008
  • Journal Name: Pakistan Journal of Medical Sciences
  • Journal Indexes: Scopus
  • Page Numbers: pp.471-474
  • Keywords: Alkaline phosphatase, Hydatidiform mole, Ion exchange
  • Kocaeli University Affiliated: Yes

Abstract

Objective: Study was performed on purification of alkaline phosphatase from Hydatiform mole. Methodology: 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 G200, Ion exchange chromatography and preparative electrophoresis. Results: 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. Conclusion: Human Hydatidiform mole alkaline phosphatase is a novel alkaline phosphatase.