title: Purification of human serum vitamin D-binding protein by 25-hydroxyvitamin D3-Sepharose chromatography.
abstract: 25-Hydroxyvitamin D3-Sepharose was prepared by coupling 25-hydroxyvitamin D3-3 beta-(1,2-epoxypropyl)-ether to thio-activated Sepharose CL-6B, forming a protease-resistant linkage between the sterol and the matrix. Vitamin D-binding protein from human plasma was obtained 85-92% pure after ligand affinity chromatography. Subsequent hydroxylapatite chromatography provided homogeneous protein. The purified vitamin D-binding protein was fully active in regard to 25-hydroxyvitamin D3 and actin binding capabilities.
mesh_terms: D002112:Calcifediol; D002846:Chromatography, Affinity; D006801:Humans; D012685:Sepharose; D014809:Vitamin D-Binding Protein / Q000097:blood*
chemical_list: D014809:Vitamin D-Binding Protein; D012685:Sepharose; D002112:Calcifediol