[Isolation and comparative characteristics of rat transcortin in normal conditions and during experimental circulatory insufficiency].
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.
Nadol'nik
L I
LI
Galitskiĭ
E A
EA
Beluga
V V
VV
Vinogradov
V V
VV
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
D014156:Transcortin
Vydelenie i sravnitel'naia kharakteristika transkortina krysy v norme i pri éksperimental'noĭ nedostatochnosti krovoobrashcheniia.