[Isolation and characterization of the placental protein pp5 (author's transl)]

Abstract

The isolation and characterization of placemental protein PP5 is described. The purification was achieved by use of immunoadsorbents. From the tissue of one human term placenta an average amount of 15 mg PP5 can be extracted. PP5 apparently is specific for the placenta; it could not be detected in extracts from other human tissues. In sera from pregnant women PP5 is not present or only in trace amounts (less than 0.1 mg%). In the ultracentrifuge PP5 was found to have a sedimentation coefficient of 2.8 S and a molecular weight of 36,600 daltons. Electrophoretically the protein migrates as a fast beta1-globulin. The isoelectric point was determined to be 4.6. PP5 is a glycoprotein and contains 19.8% carbohydrates (hexoses 10.0%, hexosamine 4.4%, fucose 0.4%, sialic acid 5.0%). The amino acid composition of the protein is reported, too. PP5 was found to inhibit the activity of trypsin and plasmin; the biological role of this protein therefore may be the inhibition of proteases.