title: Inverse stereoselectivity in the binding of acenocoumarol to human serum albumin and to alpha 1-acid glycoprotein.
abstract: Stereoselective binding of rac-acenocoumarol to human serum albumin (HSA) and alpha 1-acid glycoprotein (alpha 1-AGP) was investigated by affinity chromatography and by combined ultrafiltration (UF) and circular dichroism (CD) methods. For HSA, the ratio of the enantiomeric constants was KR/KS = 2, while for alpha 1-AGP, KS/KR = 3.
authors.affiliation: Central Research Institute for Chemistry, Hungarian Academy of Sciences, Budapest.
authors.forename: I
authors.initials: I
authors.lastname: Fitos
authors.forename: J
authors.initials: J
authors.lastname: Visy
authors.forename: A
authors.initials: A
authors.lastname: Magyar
authors.forename: J
authors.initials: J
authors.lastname: Kajtár
authors.forename: M
authors.initials: M
authors.lastname: Simonyi
mesh_terms: D000074:Acenocoumarol / Q000097:blood*; D002846:Chromatography, Affinity; D002942:Circular Dichroism; D006801:Humans; D009961:Orosomucoid / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013237:Stereoisomerism; D014462:Ultrafiltration
chemical_list: D009961:Orosomucoid; D012709:Serum Albumin; D000074:Acenocoumarol