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1: Protein Expr Purif. 1995 Apr;6(2):185-8.Click here to read Links

Affinity purification of human plasma vitamin D-binding protein.

Department of Medicine, Boston University Medical Center, Massachusetts 02118, USA.

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.

PMID: 7606167 [PubMed - indexed for MEDLINE]