Human Bone Morphogenetic Protein (hBMP)

Marshall R. Urist; Keiji Sato; Anna G. Brownell; Theodore I. Malinin; Arthur Lietze; Yong Kang Huo; Donald J. Prolo; Sally Oklund; Gerald A.M. Finerman; Robert J. Delange

doi:10.3181/00379727-173-41630

Human Bone Morphogenetic Protein (hBMP)

Marshall R. Urist, Keiji Sato, Anna G. Brownell, Theodore I. Malinin, Arthur Lietze, Yong Kang Huo, Donald J. Prolo, Sally Oklund, Gerald A.M. Finerman, Robert J. Delange

Orthopaedics

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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.

Original language	English (US)
Pages (from-to)	194-199
Number of pages	6
Journal	Proceedings of the Society for Experimental Biology and Medicine
Volume	173
Issue number	2
DOIs	https://doi.org/10.3181/00379727-173-41630
State	Published - Jun 1983

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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

Human Bone Morphogenetic Protein (hBMP). / Urist, Marshall R.; Sato, Keiji; Brownell, Anna G.; Malinin, Theodore I.; Lietze, Arthur; Huo, Yong Kang; Prolo, Donald J.; Oklund, Sally; Finerman, Gerald A.M.; Delange, Robert J.

In: Proceedings of the Society for Experimental Biology and Medicine, Vol. 173, No. 2, 06.1983, p. 194-199.

Research output: Contribution to journal › Article

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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.",

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AU - Sato, Keiji

AU - Brownell, Anna G.

AU - Malinin, Theodore I.

AU - Lietze, Arthur

AU - Huo, Yong Kang

AU - Prolo, Donald J.

AU - Oklund, Sally

AU - Finerman, Gerald A.M.

AU - Delange, Robert J.

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AB - 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.

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