Collagen Corporation

Thomas Thomas

Saeid Seyedin

Hanne Bentz

Rosa Armstrong

Larry Ellingsworth

Two proteins that are found in bone and that have in vivo chondrogenic/osteogenic activity in combination with a co-factor are described. Both proteins also were active in combination with EGF in the in vitro TGF-.beta. assay. Each has a molecular weight of approximately 26,000 daltons by SDS-PAGE. Each is reduced to a single polypeptide indicating that the proteins are probably homodimers. One has an N-terminal sequence identical to that of human placenta-derived TGF-.beta. whereas the other has an N-terminal sequence that is different from that of TGF-.beta. derived from human placenta. The two proteins may be purified to hmogeneity using RP-HPLC or acetic acid-urea gel electrophoresis.

Polypeptide cartilage-inducing factors found in bone

Two proteins that are found is bone and that have in vivo chondrogenic/osteogenic activity in combination with a co-factor are described. Both proteins also were active in combination with EGF in the in vitro TGF-.beta. assay. Each has a molecular weight of approximately 26,000 daltons by SDS-PAGE. Each is reduced to a single polypeptide indicating that the proteins are probably homodimers. One has an N-terminal sequence identical to that of human placenta-derived TGF-.beta. whereas the other has an N-terminal sequence that is different from that of TGF-.beta. derived from human placenta. The two proteins may be purified to homogeneity using RP-HPLC or acetic acid-urea gel electrophoresis.

Two proteins that are found in bone and that have in vivo chondrogenic/osteogenic activity in combination with a co-factor are described. Both proteins also were active in combination with EGF in the in vitro TGF-.beta. assay. Each has a molecular weight of approximately 26,000 daltons by SDS-PAGE. Each is reduced to a single polypeptide indicating that the proteins are probably homodimers. One has an N-terminal sequence identical to that of human placenta-derived TGF-.beta. whereas the other has an N-terminal sequence that is different from that of TGF-.beta. derived from human placenta. The two proteins may be purified to homogeneity using RP-HPLC or acetic acid-urea gel electrophoresis.

Polypeptide cartilage-inducing factors found in bone used in tissue

A partially purified proteinaceous bone-inducing factor of 10,000 to 30,000 daltons is described. It is derived from demineralized bovine bone by extraction with a chaotropic agent, gel filtration, cation exchange chromatography using carboxymethyl cellulose at pH 4.8 and gradient elution with NaCl at 10 mM to about 150 mM.

Partially purified bone-inducing factor

A process for partially purifying an osteogenic factor from demineralized bone particles in which nonfibrous proteins are extracted from the demineralized bone with a dissociative extractant for nonfibrous proteins, such as urea or guanidine hydrochloride, the extracted nonfibrous proteins are fractionated by anion exchange chromatography using DEAE cellulose at pH 7, the fraction not adsorbed by the DEAE cellulose is further fractionated by cation exchange chromatography using CM cellulose at pH 4.8, the fraction adsorbed by the CM cellulose is eluted therefrom and the partially purified osteogenic factor is recovered from the eluate as a .ltoreq.30,000 dalton protein isolate.

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Davis, CA, United States of America

Thomas Thomas