title: Progesterone binding to the tryptophan residues of human alpha1-acid glycoprotein.
abstract: Binding studies between progesterone and alpha1-acid glycoprotein allowed us to demonstrate that the binding site of progesterone contains one hydrophobic tryptophan residue and that the structure of the protein is not altered upon binding. The data obtained at saturated concentrations of progesterone clearly reveal the type of interaction at physiological levels.
authors.affiliation: Laboratoire de Biophysique Moléculaire, Université des Sciences et Technologies de Lille, Bât. C6. 59655 Villeneuve d'Ascq Cédex, France. Jihad-Rene.Albani@univ-lille1.fr
authors.forename: J R
authors.initials: JR
authors.lastname: Albani
mesh_terms: D001665:Binding Sites; D001798:Blood Proteins / Q000737:chemistry*; D006023:Glycoproteins / Q000737:chemistry*; D006801:Humans; D009961:Orosomucoid / Q000737:chemistry*; D011374:Progesterone / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D014364:Tryptophan
chemical_list: D001798:Blood Proteins; D006023:Glycoproteins; D009961:Orosomucoid; D011374:Progesterone; D014364:Tryptophan