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Bone morphogenetic protein (BMP) was extracted from human dentin matrix with 4 mol/L guanidine-HCl and was purified by liquid chromatography. SDS-PAGE and IEF showed that the purified BMP was homogeneous and induced new bone formation in situ after three weeks when implanted into muscle pouches in Wistar rats. The molecular weight of BMP was estimated to be about 20.0 kDa by SDS-PAGE, and the pI value was 8.8 by IEF. Amino acid analysis suggested that BMP is a protein containing 191 amino acids. A partial amino acid sequence was obtained from the final purified BMP. Dentin-matrix-derived BMP is probably not identical to, but is similar to, bone-matrix-derived BMP, though both types of BMP have the same action in vivo.
Bessho et al. (Fri,) studied this question.