Abstract
An bovine, amniotic-fluid protein, (bAP), was purified from amniotic fluid by gel filtration, anion exchange chromatography and isoelectric focusing. The isolation was monitored by a double immunodiffusion with an antiserum raised against amniotic fluid antigens and absorbed with maternal and fetal sera. The molecular weight of an amniotic fluid protein isolated was estimated as 60, 000 by SDS-PAGE, and the isoelectric point by isoelectric focusing was 3.4-3.8.