[New placental protein (PP15) with immunosuppressive properties (author's transl)]

The isolation and characterization of a new placental protein (PP15) which has immunosuppressive properties are described. The protein was purified from extracts of human term placentae by rivanol and ammonium sulfate fractionation, gel filtration, ion exchange chromatography, preparative zone electrophoresis, and chromatography on hydroxyapatite. PP15 was found to have a sedimentation coèfficient of 2.9 S and a molecular weight of 30,700 daltons as determined by ultracentrifugation; its molecules apparently are composed of two identical subunits which are held together by non-covalent bonds. The electrophorectic mobility of PP15 corresponds to that of albumin. PP15 is a glycoprotein and contains 3.3% carbohydrates (hexoses 2.8%, hexosamines 0.3%, sialic acid 0.2%). The amino acid composition of this protein was also determined: the most abundant amino acids in the peptide chain were found to be glutamic acid, aspartic acid, isoleucine, and leucine. PP15 has immunosuprressive properties: on testing its effect on the lymphoycte transformation in the MLC-test in vitro a significant inhibitory activity could be demonstrated.