title: A glycosylated prolactin species is covalently bound to immunoglobulin in human amniotic fluid.
abstract: Western immunoblots performed during separation of glycosylated prolactin from amniotic fluid revealed that some of the glycosylated prolactin is covalently bound to another protein. Using high performance liquid chromatography and other protein isolation techniques we have demonstrated that a glycosylated prolactin species is linked to immunoglobulin by disulfide bonds in amniotic fluid.
authors.affiliation: Department of Obstetrics, Gynecology and Reproductive Biology, Brigham and Women's Hospital, Boston, MA.
authors.forename: L J
authors.initials: LJ
authors.lastname: Heffner
authors.forename: L S
authors.initials: LS
authors.lastname: Gramates
authors.forename: R W
authors.initials: RW
authors.lastname: Yuan
mesh_terms: D000653:Amniotic Fluid / Q000032:analysis* / Q000276:immunology; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D015151:Immunoblotting; D007128:Immunoglobulin Fragments / Q000302:isolation & purification; D007136:Immunoglobulins / Q000145:classification / Q000302:isolation & purification*; D008970:Molecular Weight; D011247:Pregnancy; D011388:Prolactin / Q000276:immunology / Q000302:isolation & purification / Q000031:analogs & derivatives; D011485:Protein Binding
chemical_list: D007128:Immunoglobulin Fragments; D007136:Immunoglobulins; C043928:prolactin, glycosylated; D011388:Prolactin