The objective of this study was to develop an efficient method for the production of bioactive bone morphogenetic protein 2 (BMP-2). A recombinant plasmid encoding mature human BMP-2 was transferred and expressed at a high level in E.coli. Most of the aimed proteins existed in inclusion bodies. The non-active recombinant human BMP-2 (rhBMP-2) monomer in inclusion bodies was refolded and simultaneously purified using hydroxyapatite (HA) chromatography. After oxidization of the monomer, the rhBMP-2 dimmer showed biological activity by the induction of alkaline phosphate activity in C2C12 cells. The refolding yield was about 30% and the purity was about 90% just by one chromatography process.