Bovine Collagen Modified by PEG

  • W. Rhee
  • J. Carlino
  • S. Chu
  • H. Higley
Part of the Topics in Applied Chemistry book series (TAPP)


Currently much interest has been shown in attaching poly(ethylene glycol) (PEG) to proteins as a means of increasing solubility and serum lifetime.1–3 Modification of proteins by PEG has been used to reduce the immunogenicity of various enzymes.4–6 PEG is well known to be nontoxic, nonantigenic, biocompatible, and soluble in water and organic solvents.7–9


Fibrillar Collagen Extrusion Force Bovine Collagen Porcine Dermis Soft Tissue Augmentation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    J. M. Harris, J. Macromol. Sci., Rev. Macromol. Chem. Phys. C25, 325 (1985).CrossRefGoogle Scholar
  2. 2.
    B. Z. Weiner and A. Zilkha, J. Med. Chem. 16, 573 (1973).PubMedCrossRefGoogle Scholar
  3. 3.
    N. V. Katre, M. J. Knauf, and W. J. Laird, Proc. Natl. Acad. Sci. U.S.A. 84, 1487 (1987).PubMedCrossRefGoogle Scholar
  4. 4.
    A. Abuchowski, T. van Es, N. C. Palczuk, and F. F. Davis, J. Biol. Chem. 252, 3578 (1977).PubMedGoogle Scholar
  5. 5.
    A. Abuchowski, J. R. McCoy, N. C. Palczuk, T. van Es, and F. F. Davis, J. Biol. Chem. 252, 3582 (1977).PubMedGoogle Scholar
  6. 6.
    Y. Ashihara, T. Kona, S. Yamazaki, and Y. Inada, Biochem. Biophys. Res. Commun. 83, 385 (1978).PubMedCrossRefGoogle Scholar
  7. 7.
    K. Soehring, K. Scriba, M. Frahm, and G. Zollner, Arch. Int. Pharmacodyn. Ther. 87, 301 (1951).PubMedGoogle Scholar
  8. 8.
    C. G. Hunter, D. E. Stevenson, and P. L. Chambers, Food Cosmet. Toxicol. 5, 195 (1967).PubMedCrossRefGoogle Scholar
  9. 9.
    H. F. Smyth, Jr., C. P. Carpenter, and C. S. Weil, J. Am. Pharm. Assoc. 44, 27 (1955).Google Scholar
  10. 10.
    A. Kligman and B. Pharriss (eds.), Symposium on Injectable Collagen Implants, J. Dermatol. Surg. Onc. 14, 1 (1988).Google Scholar
  11. 11.
    F. DeLustro, S. T. Smith, J. Sundsmo, G. Salem, S. Kincaid, and L. Ellingsworth, Plast. Reconstr. Surg. 79(4), 581 (1987).PubMedCrossRefGoogle Scholar
  12. 12.
    J. M. McPherson, D. G. Wallace, A. M. Conti, S. Sawamura, R. A. Condell, S. Wade, and K. A. Piez, Collagen Rel. Res. 5, 199 (1985).CrossRefGoogle Scholar
  13. 13.
    D. G. Wallace and A. Thompson, Biopolymers 22, 1793 (1983).PubMedCrossRefGoogle Scholar
  14. 14.
    J. M. McPherson, P. W. Ledger, S. Sawamura, A. M. Conti, S. Wade, H. Reihanian, and D. G. Wallace, J. Biomed. Mater. Res. 20, 79 (1986).PubMedCrossRefGoogle Scholar
  15. 15.
    A. Finch and D. A. Ledward, Biochem. Biophys. Acta 278, 433 (1972).PubMedCrossRefGoogle Scholar
  16. 16.
    F. Flandin, C. Buffevant, and D. Herbage, Biochem. Biophys. Acta 791, 205 (1984).PubMedCrossRefGoogle Scholar
  17. 17.
    D. A. Wallace, R. A. Condell, J. W. Donovan, A. Paivinen, W. M. Rhee, and S. B. Wade, Biopolymers 25, 1875 (1986).PubMedCrossRefGoogle Scholar
  18. 18.
    A. F S. A. Habeeb, Anal. Biochem. 14, 328 (1966).PubMedCrossRefGoogle Scholar
  19. 19.
    M. L. Kakade and I. E. Liener, Anal. Biochem. 27, 273 (1969).PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1992

Authors and Affiliations

  • W. Rhee
    • 1
  • J. Carlino
    • 2
  • S. Chu
    • 2
  • H. Higley
    • 2
  1. 1.Research and DevelopmentCollagen CorporationPalo AltoUSA
  2. 2.Celtrix LaboratoriesPalo AltoUSA

Personalised recommendations