title: [Isolation and comparative characteristics of rat transcortin in normal conditions and during experimental circulatory insufficiency].
abstract: Corticosteroid binding protein, transcortin, was isolated using biospecific and hydroxyapatite chromatographic procedures. Mr-60,000 of transcortin was evaluated by means of electrophoresis; isoelectric points of the protein and of its complexes were detected. The association constants of transcortin with cortisol at 4 degrees constituted 2.8.10(8) M-1/mol of protein from intact animals containing one binding site and 9.8.10(8) M-1/mol of protein from impaired rates containing 0.39 binding site per a molecule. The maximal cortisol-binding activity of transcortin was shifted towards more alkaline pH value under the pathological conditions. Circular dichroism spectra of the transcortin-cortisol equimolar complexes were studied. The proteins studied were dissimilar in their main physicochemical properties and patterns of the steroid binding.
authors.forename: L I
authors.initials: LI
authors.lastname: Nadol'nik
authors.forename: E A
authors.initials: EA
authors.lastname: Galitskiĭ
authors.forename: V V
authors.initials: VV
authors.lastname: Beluga
authors.forename: V V
authors.initials: VV
authors.lastname: Vinogradov
mesh_terms: D000818:Animals; D002318:Cardiovascular Diseases / Q000097:blood*; D002846:Chromatography, Affinity; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D011485:Protein Binding; D051381:Rats; D014156:Transcortin / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D014156:Transcortin
vernacular_title: Vydelenie i sravnitel'naia kharakteristika transkortina krysy v norme i pri éksperimental'noĭ nedostatochnosti krovoobrashcheniia.