title: [Study of soluble proteins from human amniotic fluid by fraction chromatography (author's transl].
abstract: The nature and origin of soluble proteins from human amniotic fluid have been investigated by gel filtration chromatography on Sepharose 6B and ion-exchange chromatography on Ecteola-cellulose. Each fraction has been studied by immunoelectrophoresis. Specific antisera against serum proteins, amniotic fluid proteins, fetal proteins and salivary proteins have been used. These various antisera showed that the amniotic fluid contains maternal proteins, but also more specific proteins from fetal origin such as beta2-microglobulin, urinary mucopolysaccharides, salivary proteins and carcinoembryonic antigen. These results not only confirm that amniotic proteins are essentially from maternal origin, but prove the important fetal contribution and emphasize the importance of the fetoplacental unit in the monitoring of high risk pregnancies.
mesh_terms: D000653:Amniotic Fluid / Q000032:analysis*; D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004586:Electrophoresis; D005260:Female; D005326:Fetal Proteins / Q000032:analysis; D006025:Glycosaminoglycans / Q000032:analysis; D006801:Humans; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D011247:Pregnancy; D011506:Proteins / Q000032:analysis*; D011817:Rabbits / Q000276:immunology; D012995:Solubility
chemical_list: D005326:Fetal Proteins; D006025:Glycosaminoglycans; D011506:Proteins
vernacular_title: Etude des constituants prot:eiques du liquide amniotique apr:es fractionnement chromatographique.