Studies on bone morphogenetic protein(BMP) derived from bovine demineralized dentin matrix.

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Bone morphogenetic protein derived from bovine decalcified dentin matrix (d-BMP) has been solubilized with 4M guanidine hydrochrolide (GuHC1) and purified. It was insoluble in 0.01M CH<SUB>3</SUB>COONa containing 6M urea (pH 4.8), 0.5M GuHCl and water. The solubilized fractions were purified by 2 steps of gel filtration on Superose 12 following Sephacryl S-200, and by anion exchange chromatography on Mono Q HR 5/5. The activity of d-BMP was bioassayed by implantation in AKR mouse thigh muscle, and observed both radiologically and histologically. The final purificates indicated its molecular weight to be about 26 K daltons on SDS-PAGE and 29 K daltons after reduction with 2-mercaptoethanol. Isoelectric point was about 6.5 on isoelectric focusing. By amino acid analysis, the prominent amino acids were Asp, Tyr, Glu and Ser. The biochemical characteristics of d-BMP seemed to be different from other previously reported BMP, even BMP derived from bovine decalcified bone matrix. It suggests that possibility BMP differs in various tissues even in the same species.
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