Recombinant expression of mouse osteocalcin protein in Escherichia coli
| Autor: | Ji-Hyun Kim, Jun-Hyeog Jang, Soonok Park, Hae-Won Kim |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
musculoskeletal diseases
Osteocalcin Bioengineering Plasma protein binding medicine.disease_cause Applied Microbiology and Biotechnology law.invention Mice law Cell Adhesion Escherichia coli medicine Animals Cell adhesion Cells Cultured Osteoblasts biology Osteoblast General Medicine Alkaline Phosphatase biology.organism_classification Enterobacteriaceae Recombinant Proteins Durapatite medicine.anatomical_structure Biochemistry Recombinant DNA biology.protein Alkaline phosphatase Protein Binding Biotechnology |
| Zdroj: | Biotechnology Letters. 29:1631-1635 |
| ISSN: | 1573-6776 0141-5492 |
| DOI: | 10.1007/s10529-007-9437-z |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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