Prion protein (PrPc) interacts with histone H3 confirmed by affinity chromatography

被引:3
作者
Cai, Hanning [1 ]
Xie, Ying [1 ]
Hu, Lingyin [1 ]
Fan, Jingjing [1 ]
Li, Renqiang [1 ]
机构
[1] Jinan Univ, Dept Biotechnol, Guangzhou 510632, Guangdong, Peoples R China
来源
JOURNAL OF CHROMATOGRAPHY B-ANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL AND LIFE SCIENCES | 2013年 / 929卷
关键词
Prion protein; Histone H3; Interaction; Affinity chromatography; CHROMATIN; EXPRESSION;
D O I
10.1016/j.jchromb.2013.04.003
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The histones including H2a, H2b, H3 and H4 purified from pig liver tissue were immobilized onto Sepharose 4B to create a histone-Sepharose column. During chromatography of cow milk casein by histone-Sepharose column, two isoforms of prion protein (PrPc) with 34 and 30 kDa molecular mass corresponding to diglycosylated and monoglycosylated PrPc respectively were found to be captured by histone ligands. To further verify the interaction between histones and PrPc, the PrPc-Sepharose column was prepared and used to separate the histones. Two chromatography processes and SOS-PAGE demonstrated that only H3 in the histones was found to interact with PrPc. This study suggested H3 could be the target molecule of PrPc in nuclei, which might be useful for understanding the prion disease. (C) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码:40 / 44
页数:5
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