Binding of 17beta-estradiol by variants of alpha-fetoprotein in rat amniotic fluid.
Two variants of alpha-fetoprotein in rat amniotic fluid were separated by their different affinity for concanavalin A-Sepharose, which selectively binds alpha-D-manno-pyranosides and alpha-D-glucopyranosides. Both forms had the same mobility upon polyacrylamide gel electrophoresis. The binding of 17beta-estradiol per mg of alpha-fetoprotein, determined both immunologically and electrophoretically, was the same for both variants. These results indicate that a specific carbohydrate portion of the molecule is not necessary for steroid binding.
D000653:Amniotic Fluid / Q000032:analysis*; D000818:Animals; D001665:Binding Sites; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004958:Estradiol; D005260:Female; D005326:Fetal Proteins / Q000302:isolation & purification; D009439:Neuraminidase; D011247:Pregnancy; D011485:Protein Binding; D051381:Rats; D000509:alpha-Fetoproteins / Q000302:isolation & purification
D005326:Fetal Proteins; D000509:alpha-Fetoproteins; D004958:Estradiol; D009439:Neuraminidase