| Autor: |
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. |
| Zdroj: |
Experimental Biology and Medicine; June 1983, Vol. 173 Issue: 2 p194-199, 6p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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