Recombinant expression of mouse osteocalcin protein in Escherichia coli

被引：14
|
作者：
Kim, Ji-Hyun
Park, Soonok
Kim, Hae-Won
Jang, Jun-Hyeog [1 ]
机构：
[1] Inha Univ, Coll Med, BK21 Ctr Adv Med Educ, Dept Biochem, Inchon 400712, South Korea
[2] Dankook Univ, Sch Dent, Dept Biomat Sci, Omiya, Saitama 330, Japan
来源：
BIOTECHNOLOGY LETTERS | 2007年 / 29卷 / 11期
关键词：
bone; cell adhesion; extracellular matrix; osteoblast; osteocalcin;
D O I：
10.1007/s10529-007-9437-z
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
Osteocalcin is the most abundant non-collagenous protein of bone. Recombinant mouse osteocalcin protein (mOC) that includes the highly conserved central domain for binding to hydroxyapatite (HA), a mineral component of bone, was expressed in Escherichia coli. Purified mOC protein exhibited a significant increase in HA adhesion and differentiation in osteoblast cells as well as binding to HA with high affinity.
引用
收藏
页码：1631 / 1635
页数：5
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