Oestriol binding to plasma proteins.
Simple diffusion experiments indicated that oestriol was retained by human pregnancy plasma more effectively than by albumin solutions of a corresponding concentration. Oestriol bound (Ka = 6 X 10(6) l/mol at 4 degrees C) to a glycoprotein which had been isolated from plasma by adsorption to Concanavalin A. The free energy of binding at 37 degrees C was -38 kJ/mol. Competition experiments indicated that the oestriol binding glycoprotein had properties expected of sex hormone binding globulin. The distribution of oestriol among the protein fractions of human pregnancy plasma--glycoprotein bound 7.8%, albumin bound 78.6%, unbound 13.6%--suggests that this glycoprotein plays little part in the transport of oestriol.
Moutsatsou
V
V
Department of Chemical Pathology, School of Medicine, University of Leeds, England.
Oakey
R E
RE
D001667:Binding, Competitive; D001798:Blood Proteins / Q000378:metabolism*; D004958:Estradiol / Q000097:blood; D004964:Estriol / Q000097:blood*; D005260:Female; D006023:Glycoproteins / Q000097:blood; D006801:Humans; D011247:Pregnancy / Q000097:blood*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism; D013816:Thermodynamics
D001798:Blood Proteins; D006023:Glycoproteins; D012709:Serum Albumin; D004958:Estradiol; D004964:Estriol