U.S. patents available from 1976 to present.
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Polypeptide cartilage-inducing factors found in bone

Patent 4774322 Issued on September 27, 1988. Estimated Expiration Date: Icon_subject December 10, 2007. Estimated Expiration Date is calculated based on simple USPTO term provisions. It does not account for terminal disclaimers, term adjustments, failure to pay maintenance fees, or other factors which might affect the term of a patent.

Patent References

Bone morphogenetic protein process
Patent #: 4294753
Issued on: 10/13/1981
Inventor: Urist

Partially purified osteogenic factor and process for preparing same from demineralized bone
Patent #: 4434094
Issued on: 02/28/1984
Inventor: Seyedin ,   et al.

Inductive collagen based bone repair preparations Patent #: 4563350
Issued on: 01/07/1986
Inventor: Nathan ,   et al.

Inventors

Assignee

Application

No. 07/129864 filed on 12/10/1987

US Classes:

530/353, Scleroproteins, e.g., fibroin, elastin, silk, etc.514/21, Produced by or extracted from animal tissue530/350, PROTEINS, I.E., MORE THAN 100 AMINO ACID RESIDUES530/840, Bones; tendons; teeth; cartilage623/924, MATERIAL CHARACTERISTIC930/120Growth hormone, growth factor other than T-cell or B-cell growth factor, and growth hormone releasing factor; related peptides

Examiners

Primary: Phillips, Delbert R.
Assistant: Nutter, Nathan M.

Attorney, Agent or Firm

International Classes

A61L 27/00 (20060101)
A61L 27/22 (20060101)
C07K 14/435 (20060101)
C07K 14/495 (20060101)
A61K 38/00 (20060101)

Foreign Application Priority Data

1985-07-08 EP

Abstract

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-ଲ 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-ଲ whereas the other has an N-terminal sequence that is different from that of TGF-ଲ derived from human placenta. The two proteins may be purified to homogeneity using RP-HPLC or acetic acid-urea gel electrophoresis.

Other References

  • Cytokine Bulletin, vol. 1, No. 1, Jan. 1987
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  • Termine et al., "Mineral and Collagen-binding Proteins of Fetal Calf Bone", Journal of Biological Chemistry, vol. 221, No. 20, pp. 10403-10408, 1981
  • Assoian et al, "Transforming Growth Factor-ଲ in Human Platelets, Identification of a Major Storage Site Purification, and Characterization", Journal of Biological Chemistry, vol. 258, No. 11, pp. 7155-7160, 1983
  • Seyedin et al., "Cartilage-inducing Factor A-Apparent Identity to Transforming Growth Factor-ଲ", Journal of Biological Chemistry vol. 261, No. 13, pp. 5693-5695, 1986
  • Urist, et al., Clinical Orthopaedics and Related Research (1982) No. 162, Jan., Feb., pp. 219-232
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  • Roberts, A. B., et al., Proc Natl Acad Sci (USA) (9185) 82:119-123
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