title: Effects of drug-binding on the thermal denaturation of human serum albumin.
abstract: Asymmetric thermograms of defatted albumin, alone and in the presence of two model drugs, have been obtained in phosphate buffers at three pH values. The albumin is less thermally stable in the N form, but is protected by both drugs. The nonsteroidal antiinflammatory benoxaprofen offers more protection than warfarin against thermal denaturation.
authors.affiliation: Department of Comparative and Experimental Pathology, University of Florida, Gainesville 32610, USA.
authors.forename: K
authors.initials: K
authors.lastname: Lohner
authors.forename: A C
authors.initials: AC
authors.lastname: Sen
authors.forename: R
authors.initials: R
authors.lastname: Prankerd
authors.forename: A F
authors.initials: AF
authors.lastname: Esser
authors.forename: J H
authors.initials: JH
authors.lastname: Perrin
mesh_terms: D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000494:pharmacology*; D001665:Binding Sites; D002152:Calorimetry, Differential Scanning; D006801:Humans; D011422:Propionates / Q000494:pharmacology*; D011489:Protein Denaturation; D012709:Serum Albumin / Q000737:chemistry*; D014859:Warfarin / Q000494:pharmacology*
chemical_list: D000894:Anti-Inflammatory Agents, Non-Steroidal; D011422:Propionates; D012709:Serum Albumin; C011677:benoxaprofen; D014859:Warfarin