Purification and characterization of a bone-inducing protein from a murine osteosarcoma (Dunn type).
A protein fraction capable of eliciting cartilage or bone formation in vivo was purified more than 100,000-fold from a murine osteosarcoma (Dunn type). Intramuscular implantation of as little as 20 ng of the purified protein with 2 mg of pure skin collagen consistently induced ectopic new bone formation. The apparent molecular size of the purified protein was 32 kd on sodium dodecylsulfate-polyacrylamide gel electrophoresis. On reduction, the 32-kd protein split into subunits with the same partial amino acid sequences, and these partial sequences were identical to those of human bone morphogenetic protein-2B (BMP-4) which is assumed to be a member of the transforming growth factor-beta superfamily.
Department of Orthopaedic Surgery, Osaka University Medical School, Japan.
K
K
Takaoka
H
H
Yoshikawa
J
J
Hashimoto
S
S
Miyamoto
K
K
Masuhara
H
H
Nakahara
M
M
Matsui
K
K
Ono
D000595:Amino Acid Sequence; D000818:Animals; D001681:Biological Assay; D019485:Bone Morphogenetic Proteins; D004591:Electrophoresis, Polyacrylamide Gel; D051379:Mice; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000737:chemistry / Q000302:isolation & purification*; D012516:Osteosarcoma / Q000378:metabolism; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification*; D014407:Tumor Cells, Cultured
D019485:Bone Morphogenetic Proteins; D009363:Neoplasm Proteins; D011506:Proteins