CRYSTALLIZATION AND X-RAY-INVESTIGATION OF VITAMIN-D-BINDING PROTEIN FROM HUMAN SERUM - IDENTIFICATION OF THE CRYSTAL CONTENT

被引：14
作者：
VERBOVEN, CC
DEBONDT, HL
DERANTER, C
BOUILLON, R
VANBAELEN, H
机构：
[1] KATHOLIEKE UNIV LEUVEN,FAC FARMACEUT WETENSCHAPPEN,ANALYT CHEM & MED FYSICOCHEM LAB,B-3000 LOUVAIN,BELGIUM
[2] LAB EXPTL GENEESKUNDE & ENDOCRINOL ONDERWIJS & NA,B-3000 LOUVAIN,BELGIUM
来源：
JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY | 1995年 / 54卷 / 1-2期
关键词：
D O I：
10.1016/0960-0760(95)00123-H
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Vitamin D-binding protein (DBP), a multifunctional, highly polymorphic glycoprotein responsible for the transport of vitamin D and for sequestering extracellular actin, was isolated from human serum and crystallized using vapour diffusion methods. The crystals were grown from 7.5% v/v polyethylene glycol 400 and 0.1 M acetate buffer at pH 4.6. These crystals show diffraction patterns consistent with the tetragonal space groups P4(1), and P4(3) with unit cell dimensions a = b = 135.5(4) Angstrom and c =75.9(4) Angstrom. They diffract to 2.3 Angstrom Using polyacrylamide gel electrophoresis it was shown that according to their electrophoretic mobility the O-glycosylated isoforms, with a terminal sialic acid residue, are absent in the crystals.
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页码：11 / 14
页数：4
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