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Human bone morphogenetic protein (hBMP).

M R Urist, K Sato, A G Brownell

    Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.)
    |June 1, 1983
    PubMed
    Summary
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    Researchers isolated human bone morphogenetic protein (hBMP) from bone matrix. The 17-kDa hBMP component showed reduced bone formation compared to mixed protein fractions, suggesting other components are crucial for optimal bone regeneration.

    Area of Science:

    • Biochemistry
    • Biomaterials Science
    • Orthopedic Research

    Background:

    • Human bone morphogenetic protein (hBMP) is crucial for bone regeneration.
    • Efficient extraction and characterization of hBMP are essential for therapeutic applications.

    Purpose of the Study:

    • To chemically extract and isolate human bone morphogenetic protein (hBMP) from demineralized cortical bone matrix.
    • To characterize the isolated hBMP and evaluate its bone-forming capacity.

    Main Methods:

    • Chemical extraction using a CaCl2 x urea solvent mixture.
    • Differential precipitation with guanidine hydrochloride.
    • Purification via preparative gel electrophoresis.

    Main Results:

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  • hBMP was isolated at 1 mg/kg wet weight of fresh bone.
  • The primary isolated protein had a molecular weight of 17-18 kDa and acidic polypeptide composition.
  • Implants of the 17-kDa protein showed rapid adsorption but less bone volume compared to mixed fractions (24-, 17-, and 14-kDa).
  • The 24-kDa and 14-kDa components lacked hBMP activity.

    • Conclusions:

    • The isolated 17-kDa protein alone has limited bone morphogenetic activity.
    • Bone formation kinetics and the role of carrier molecules in hBMP activity require further investigation.