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Bone morphogenetic proteins (BMP) belongs to the Transforming Grown Factor -β superfamily (TGFβ). Among this group, the recombinant human BMP-2 (rhBMP-2) has been widely investigated, because of its osteoinductive activity. There is already a commercial product based on recombinant DNA technology from Chinese hamster ovary (CHO) cells and also for research use, one expressed in the cytoplasm of Escherichia coli (E. coli). The rhBMP-2 in its homodimer form has high biological activity, lead to a bone mineralization in endochondral bones, and differentiate mesenchymal cells into osteoblasts and osteoclasts. The aim of this study consisted in obtaining the rhBMP-2 by producing in E. coli, highly purified through chromatographic techniques and with biological activity. The bacteria strains used for production were W3110 and BL21(DE), cultivated in three different expression temperatures 25 °C, 37 °C e 42 °C. Two chromatographic techniques were used for the purification of this protein from periplasmic fluid: heparin affinity and High Performance Size Exclusion Chromatography (HPSEC). The fractions collected from these purification steps led to separation of eight products characterized by polyacrylamide gel electrophoresis (SDSPAGE) and western blotting (WB). The biological activity analysis was checked by the induction at alkaline phosphatase production in mouse myoblast C2C12 cells. The analysis of the commercial products was also made with these techniques. The results showed that two among the eight purified products, obtained from BL21 in 25°C one and W3110 42°C one, exhibit high purity and biological activity.

Expressão, purificação e caracterização físico-química da rhBMP-2 (recombinante humana BMP-2)