Abstract
The syncytiotrophoblastic cells of the human placenta contain a cytoplasmic protein recognized by fluorescein-labeled transcortin-specific antibody. Purification of this protein from human placenta, by those methods employed for the purification of human plasma transcortin, yielded a protein that exhibited antigenic and biochemical similarity to plasma transcortin. Placental transcortin differs from plasma transcortin in that it has a smaller sedimentation coefficient (3S vs 3.75S) and binds cortisol less strongly. This purified protein is able to block the phytohemagglutinin response of maternal lymphocytes even more than serum transcortin. It is postulated that the biological role may be that of inhibiting the maternal cell-mediated immune response to the presence of the antigenic conceptus.