VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Isolation and comparative characteristics of rat transcortin in normal conditions and during experimental circulatory insufficiency

   
Nadol'nik L.I., Galitskii E.A., Beluga V.V., Vinogradov V.V.
PubMed Id: 3218132
Year: 1988  Volume: 34  Issue: 5  Pages: 25-30
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.
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Nadol'nik L.I., Galitskii E.A., Beluga V.V., Vinogradov V.V. (1988) Voprosy meditsinskoi khimii, 34(5), 25-30.
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