[Isolation and characterization of pregnancy associated alpha2 glycoprotein].
A method using immunoadsorbents for the isolation of pregnancy-associated alpha2-glycoprotein (alpha2-PAG) from the extract of human placentae is described. The physical properties and the chemical composition of the purified protein are determined: alpha2PAG sediments with 11,5 S, has a molecular weight of 360 000 daltons and is composed of subunits having a molecular weight of 180000, which are held together by disulfide bonds. The isoelectric point was found to be pH 4,7 and the extinction coefficient (E1%1cm) was determined to be 9,7 at 277 nm. The carbohydrate content of the molecule amounts to 12,1% (hexose 6,0%, hexosamine 3,7%, fucose 0,06%, sialic acid 2,4%). An analysis of the amino acids is reported, too. The purified alpha2PAG was used to determine the absolute concentrations of this protein in a reference standard and in sera.
D005260:Female; D006801:Humans; D007526:Isoelectric Point; D008970:Molecular Weight; D010920:Placenta / Q000032:analysis; D011247:Pregnancy; D000511:alpha-Macroglobulins / Q000302:isolation & purification*
D000511:alpha-Macroglobulins
Isolierung und Charakterisierung des schwangerschafts-assoziierten alpha2-Glykoproteins (alpha2-PAG)