Recombinant expression of mouse osteocalcin protein in Escherichia coli.
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.
Kim
Ji-Hyun
JH
Department of Biochemistry and BK21 Center for Advanced Medical Education, Inha University College of Medicine, Incheon, 400-712, Korea.
Park
Soonok
S
Kim
Hae-Won
HW
Jang
Jun-Hyeog
JH
D000469:Alkaline Phosphatase; D000818:Animals; D002448:Cell Adhesion / Q000502:physiology; D002478:Cells, Cultured; D017886:Durapatite / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D051379:Mice; D010006:Osteoblasts / Q000502:physiology; D015675:Osteocalcin / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D011485:Protein Binding; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism
D011994:Recombinant Proteins; D015675:Osteocalcin; D017886:Durapatite; D000469:Alkaline Phosphatase