| Literature DB >> 3777429 |
R P Link, K L Perlman, E A Pierce, H K Schnoes, H F DeLuca.
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.Entities:
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Year: 1986 PMID： 3777429 DOI： 10.1016/0003-2697(86)90624-x
Source DB: PubMed Journal: Anal Biochem ISSN： 0003-2697 Impact factor: 3.365