The 4 M GuHCl soluble proteins of Dunn osteosarcoma were fractionated in two steps by means of CsCl density gradient centrifugation. Further purification of bone morphogenetic protein (BMP) was accomplished by molecular sieve techniques utilizing thin-channel diafiltration (Amicon), Sepharose CL-6B and Sephacryl S-200 gel filtration. Partially purified BMP fractions were analyzed by electrophoresis on 7.5% SDS polyacrylamide gel. The molecular weight of BMP active fractions ranges from 30,000 to a few thousand daltons. BMP may be one of the two proteins of MW of 12,500 and 16,000 daltons.

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PubMedDate not supplied

Chemosterilized autolyzed antigen-extracted allogeneic (AAA) bone matrix gelatin for repair of defects from excision of benign bone tumors: a preliminary report.

In a series of 33 bone graft operations, antigen-extracted, autolyzed, allogeneic (AAA) bone matrix gelatin was substituted for autologous bone. The period of follow-up was 2.0 to 3.5 years. AAA bone gelatin was resorbed more rapidly than whole bone. AAA bone gelatin was replaced by new bone in the same intervals of time as observed with autologous bone. In treatment of bone tumors with AA bone gelatin, the results of the operation depend upon the nature of the pathologic processes in the host bed. In normal host bed, tight contact between implant and recipient bone is essential for success. The overall results of a preliminary study of 33 cases of 91% successful.

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