Placental alkaline phosphatase has a binding site for the human immunoglobulin-G Fc portion.

Affinity chromatography of human plasma on placental-alkaline-phosphatase-Sepharose columns (placental alkaline phosphatase, PLAP) yielded consistently a pure protein which was identified as IgG on the basis of electrophoretical and immunological comparisons with authentic human IgG. SDS/PAGE of the protein revealed, under reducing conditions, two polypeptides of 55 kDa and 25 kDa. The N-terminal amino acid sequence (12 residues) of the 55-kDa subunit presented high similarity (83-100%) with known sequences of immunoglobulin gamma chains. The IgG binds by its Fc portion to a fully exposed domain in the plasma-membrane-anchored PLAP. Scatchard analysis of the interaction gave a dissociation constant of 3.68 microM, a value close to those found for haematopoietic cells and syncytiotrophoblast Fc receptors. The latter was affinity purified from human placenta as the major IgG-binding component and presented cross-immunoreactivity with anti-PLAP antibodies, indicating that PLAP and the putative placental Fc receptor could be identical molecules.