Nadol'nik L I, Galitskiĭ E A, Beluga V V, Vinogradov V V
Vopr Med Khim. 1988 Sep-Oct;34(5):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.
使用生物特异性和羟基磷灰石色谱法分离了皮质类固醇结合蛋白——皮质素转运蛋白。通过电泳评估了皮质素转运蛋白的分子量为60,000；检测了该蛋白质及其复合物的等电点。在4℃下，来自完整动物且含有一个结合位点的皮质素转运蛋白与皮质醇的缔合常数为2.8×10⁸M⁻¹/摩尔蛋白质，而来自受损大鼠且每分子含有0.39个结合位点的皮质素转运蛋白与皮质醇的缔合常数为9.8×10⁸M⁻¹/摩尔蛋白质。在病理条件下，皮质素转运蛋白的最大皮质醇结合活性向更碱性的pH值偏移。研究了皮质素转运蛋白 - 皮质醇等摩尔复合物的圆二色光谱。所研究的蛋白质在其主要物理化学性质和类固醇结合模式上存在差异。
