Abstract
Human bone morphogenetic protein (hBMP) was chemically extracted from demineralized gelatinized cortical bone matrix by means of a CaCl2·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. © 1983, SAGE Publications. All rights reserved.
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CITATION STYLE
Urist, M. R., Sato, K., Brownell, A. G., Malinin, T. I., Lietze, A., Huo, Y. K., … Delange, R. J. (1983). Human Bone Morphogenetic Protein (hBMP). Proceedings of the Society for Experimental Biology and Medicine, 173(2), 194–199. https://doi.org/10.3181/00379727-173-41630
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