Human bone morphogenetic protein (hBMP).
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.
D000328:Adult; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001681:Biological Assay; D001857:Bone Matrix / Q000032:analysis*; D019485:Bone Morphogenetic Proteins; D006801:Humans; D008297:Male; D051379:Mice; D008875:Middle Aged; D008970:Molecular Weight; D010012:Osteogenesis / Q000187:drug effects; D011506:Proteins / Q000302:isolation & purification* / Q000494:pharmacology
D000596:Amino Acids; D019485:Bone Morphogenetic Proteins; D011506:Proteins