Abstract
Clinically, it would be more convenient to use recombinant than purified preparations of bone morphogenetic protein (BMP). Recently, recombinant human BMP (rhBMP) has attracted the attention of many investigators, but it has not been fully characterized. We examined the bone-inducing activity of rhBMP-2 and compared it with that of purified BMP derived from human bone matrix (phBMP). Two, 10, or 50 μ g of rhBMP-2 or phBMP was mixed with 3 mg of atelopeptide type I collagen (carrier), and specimens were implanted in the calf muscles of Wistar rats (n =5 in each group). Four weeks later, new bone had formed in all the rhBMP-2- and phBMP-implanted muscles and was visible radiographically and histologically. The quantitative analysis indicated that the activity of rhBMP-2 was less than one tenth that of phBMP. It is necessary to find out why rhBMP-2 has fewer activities than phBMP.
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