Estrogen binding properties of a haptoglobin-hemoglobin complex isolated from human fetus.
A haptoglobin-hemoglobin complex purified from human fetus was found to be able to bind estradiol in the presence of hydrogen peroxide. Bound estradiol was copurified with the complex during the purification process: ion exchange, gel filtration and hydroxyapatite chromatographies. The hormone-labelled complex was also precipitated with an anti-adult haptoglobin. The binding resisted to denaturation and solvent extraction suggesting a covalent bond between protein and hormone.
D002845:Chromatography; D004958:Estradiol / Q000378:metabolism*; D005333:Fetus / Q000032:analysis*; D006242:Haptoglobins / Q000302:isolation & purification / Q000378:metabolism*; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007163:Immunosorbent Techniques; D011485:Protein Binding
D006242:Haptoglobins; D006454:Hemoglobins; D004958:Estradiol; D006861:Hydrogen Peroxide