title: [Microcalorimetric study of the domain organization of serum albumin].
abstract: Scanning microcalorimetry was used for studying the melting of the structure of human and bovine serum albumins and their fragments. It was shown that the melting of the native structure of serum albumin observed by the excessive heat absorption is a complex process which is described by three simple transitions overlapping in temperature. This means that the serum albumin molecule consists of three more or less independent cooperative structures, domains.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002151:Calorimetry / Q000379:methods; D002417:Cattle; D006801:Humans; D011487:Protein Conformation; D012709:Serum Albumin; D012710:Serum Albumin, Bovine; D013816:Thermodynamics
chemical_list: D012709:Serum Albumin; D012710:Serum Albumin, Bovine
vernacular_title: Mikrokalorimetricheskoe issledovanie domennoĭ organizatsii syvorotochnogo al'bumina.