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. 1983 Jun;173(2):194-9.
doi: 10.3181/00379727-173-41630.

Human bone morphogenetic protein (hBMP)

M R Urist, K Sato, A G Brownell, T I Malinin, A Lietze, Y K Huo, D J Prolo, S Oklund, G A Finerman, R J DeLange

Human bone morphogenetic protein (hBMP)

M R Urist et al. Proc Soc Exp Biol Med. 1983 Jun.

Abstract

Human bone morphogenetic protein (hBMP) was chemically extracted from demineralized gelatinized cortical bone matrix by means of a CaCl2 X urea inorganic-organic solvent mixture, differential precipitation in guanidine hydrochloride, and preparative gel electrophoresis. hBMP is isolated in quantities of 1 mg/kg of wet weight of fresh bone, and has the amino-acid composition of an acidic polypeptide. The mol wt is 17 to 18 k-Da (kilodaltons). Implants of the isolated 17-kDa protein are very rapidly adsorbed and produce a smaller volume of bone than protein fractions consisting of 24-, 17-, and 14-kDa proteins. Since the isolated 24- and 14-kDA components lack hBMP activity, the kinetics of the bone morphogenetic processes including the function of other proteins as carrier molecules, await investigation.

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