Affinity purification of human plasma vitamin D-binding protein

Protein Expr Purif. 1995 Apr;6(2):185-8. doi: 10.1006/prep.1995.1023.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Calcifediol / analogs & derivatives
  • Calcifediol / metabolism
  • Chromatography, Affinity*
  • Chromatography, Liquid
  • Durapatite
  • Humans
  • Vitamin D-Binding Protein / blood
  • Vitamin D-Binding Protein / isolation & purification*


  • 3'-O-aminopropyl-25-hydroxyvitamin D3
  • Vitamin D-Binding Protein
  • Durapatite
  • Calcifediol