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

Research output: Contribution to journalArticlepeer-review

146 Scopus citations


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 languageEnglish (US)
Pages (from-to)194-199
Number of pages6
JournalProceedings of the Society for Experimental Biology and Medicine
Issue number2
StatePublished - Jun 1983

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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