High yield isolation of BMP-2 from bone and in vivo activity of a combination of BMP-2/TGF-β1.

摘要

A high-yield purification procedure for protein fractions derived from porcine bone matrix extracts is described, which has a high abundance of bone morphogenetic protein-2 (BMP-2). Naturally derived pBMP-2, ~5 μg per kilogram of porcine bone matrix, was isolated by using a 300 kDa membrane before chromatographic processing on heparin affinity media. The elution of pBMP-2 and transforming growth factor-β(1) (TGF-β(1)) revealed morphogen peaks that were unresolved on Prosep(?) medium, but resolved on hydroxyapatite medium. Antagonism was observed in animal studies when the two proteins were combined in specific doses. The TGF-β(1) fraction alone was not active in the rodent heterotopic in vivo bioassay, confirming previously obtained results.