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  • Title: Human placental alkaline phosphatase: expression in Pichia pastoris, purification and characterization of the enzyme.
    Author: Heimo H, Palmu K, Suominen I.
    Journal: Protein Expr Purif; 1998 Feb; 12(1):85-92. PubMed ID: 9473461.
    Abstract:
    The soluble form of human placental alkaline phosphatase (PLAP) was expressed in the methylotrophic yeast Pichia pastoris and the expression product was purified and characterized. Yeast-derived PLAP (yPLAP) was secreted into the medium to the level of 2 mg/liter. yPLAP displayed kinetic properties similar to those reported earlier for the membrane-bound PLAP. Purified yPLAP had specific activity of 774 U/mg and appeared in two subunit sizes, ca. 62 and 65 kDa. This difference was due to heterogenous N-glycosylation. Purified yPLAP appeared as multiple forms in isoelectric focusing in pI range of 4.2 to 5.2. The expression system is discussed in comparison to previously reported expression systems.
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