Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase.

Ítems similars

• Selectivity at the cleavage/attachment site of phosphatidylinositol-glycan anchored membrane proteins is enzymatically determined.
  per: Micanovic, R, et al.
  Publicat: (1990)
• Characterization of the phosphatidylinositol-glycan membrane anchor of human placental alkaline phosphatase.
  per: Howard, A D, et al.
  Publicat: (1987)
• Conversion of placental alkaline phosphatase from a phosphatidylinositol-glycan-anchored protein to an integral transmembrane protein.
  per: Berger, J, et al.
  Publicat: (1989)
• Aspartic acid-484 of nascent placental alkaline phosphatase condenses with a phosphatidylinositol glycan to become the carboxyl terminus of the mature enzyme.
  per: Micanovic, R, et al.
  Publicat: (1988)
• Biosynthesis of phosphatidylinositol-glycan (PI-G)-anchored membrane proteins in cell-free systems: cleavage of the nascent protein and addition of the PI-G moiety depend on the size of the COOH-terminal signal peptide.
  per: Kodukula, K, et al.
  Publicat: (1992)