Phosphoprotein phosphatase activity of the progesterone-induced purple glycoprotein of the porcine uterus. Academic Article uri icon


  • The iron-containing, progesterone-induced, purple glycoprotein from the pig uterus catalyzes the hydrolysis of phosphate groups from phosphvitin. This enzyme which can be purified in large amounts, has a pH optimum at 4.6 and an apparent Km of 0.1 mM for bound phosphate. Its Vmax with phosphvitin as substrate is about 200, moles Pi released/min/mole enzyme and is at least twenty-fold lower than its activity towards p-nitrophenylphosphate. The enzyme is activated by 2-mercaptoethanol and inhibited by molybdate, fluoride and arsenate. The resemblance of this protein to a number of other acid phosphatases of similar substrate specificity in other organisms, suggests that a broad class of such enzymes might exist in nature. 1976.

published proceedings

  • Biochem Biophys Res Commun

author list (cited authors)

  • Roberts, R. M., & Bazer, F. W.

citation count

  • 40

complete list of authors

  • Roberts, RM||Bazer, FW

publication date

  • January 1976