Lawson D E, Charman M, Wilson P W, Edelstein S
Biochim Biophys Acta. 1976 Jul 21;437(2):403-15. doi: 10.1016/0304-4165(76)90010-6.
Protein(s) have been found in a wide range of tissues which have a high affinity for 25-hydroxycholecalciferol. Of the tissues examined only erythrocytes do not have this protein. The properties of the protein have been examined and it has been found that the association constatns range from 2 - 10(9) to 5 - 10(9) M-1 and the sedimentation constants between 5.0 and 6.0 S. It was not possible to distinguish the proteins from the different tissues by their S values, mobility on gel electrophoresis or behaviour on ion-exchange chromatography. These techniques were all used, however, to show that the tissue 25-hydroxycholecalciferol binding protein is distinct from the main plasma binding protein for this steroid and from the intestinal 1,25-dihydroxycholecalciferol-binding protein. A protein has been in the plasma of rachitic animals but not of normals, which is apparently indistinguishable from this new tissue 25-hydroxycholecalciferol-binding protein. The steroid specificity of this new binding protein has been shown to be dependent upon a C-25 hydroxyl group, and an intact conjugated double bond system. Possible functions for this protein have been briefly discussed.
已在多种组织中发现了对25-羟胆钙化醇具有高亲和力的蛋白质。在所检查的组织中,只有红细胞没有这种蛋白质。已对该蛋白质的特性进行了研究,发现其结合常数范围为2×10⁹至5×10⁹M⁻¹,沉降常数在5.0至6.0 S之间。无法通过其S值、凝胶电泳迁移率或离子交换色谱行为来区分不同组织中的蛋白质。然而,所有这些技术都用于表明组织25-羟胆钙化醇结合蛋白与该类固醇的主要血浆结合蛋白以及肠1,25-二羟胆钙化醇结合蛋白不同。在佝偻病动物的血浆中发现了一种蛋白质,而正常动物血浆中没有,这种蛋白质显然与这种新的组织25-羟胆钙化醇结合蛋白无法区分。已表明这种新结合蛋白的类固醇特异性取决于C-25羟基和完整的共轭双键系统。已简要讨论了该蛋白质可能的功能。