AFFINITY PURIFICATION OF HUMAN PLASMA VITAMIN-D-BINDING PROTEIN

被引：16

作者：

SWAMY, N ^{[1
]}

ROY, A ^{[1
]}

CHANG, R ^{[1
]}

BRISSON, M ^{[1
]}

RAY, R ^{[1
]}

机构：

[1] BOSTON UNIV,MED CTR,DEPT MED,VITAMIN LAB D,BIOORGAN & PROT CHEM GRP,BOSTON,MA 02118

来源：

PROTEIN EXPRESSION AND PURIFICATION | 1995年 / 6卷 / 02期

关键词：

D O I：

10.1006/prep.1995.1023

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 D-3 and its 25-hydroxy- and 1,25-dihydroxy metabolites with a 3'-aminopropylether group, In the present study we have coupled 25-hydroxyvitamin D-3-3 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. (C) 1995 Academic Press, Inc.

引用

页码：185 / 188

页数：4

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