title: Affinity purification of human plasma vitamin D-binding protein.
abstract: During the course of our studies to probe the vitamin D ligand-binding domains of vitamin D-binding protein and vitamin D receptor, we developed a synthetic procedure to modify the 3 beta-hydroxyl group of vitamin D3 and its 25-hydroxy- and 1,25-dihydroxy metabolites with a 3'-aminopropylether group. In the present study we have coupled 25-hydroxyvitamin D3-3 beta-3'-aminopropylether to an activated Sepharose matrix. Using this stable and reusable affinity matrix we have purified human vitamin D-binding protein from human plasma to homogeneity.
authors.affiliation: Department of Medicine, Boston University Medical Center, Massachusetts 02118, USA.
authors.forename: N
authors.initials: N
authors.lastname: Swamy
authors.forename: A
authors.initials: A
authors.lastname: Roy
authors.forename: R
authors.initials: R
authors.lastname: Chang
authors.forename: M
authors.initials: M
authors.lastname: Brisson
authors.forename: R
authors.initials: R
authors.lastname: Ray
mesh_terms: D001665:Binding Sites; D002112:Calcifediol / Q000031:analogs & derivatives / Q000378:metabolism; D002846:Chromatography, Affinity; D002853:Chromatography, Liquid; D017886:Durapatite; D006801:Humans; D014809:Vitamin D-Binding Protein / Q000097:blood / Q000302:isolation & purification*
chemical_list: C094571:3'-O-aminopropyl-25-hydroxyvitamin D3; D014809:Vitamin D-Binding Protein; D017886:Durapatite; D002112:Calcifediol