Advertisement

Surface Modification of Proteins

  • Roland R. Reiner
  • Helga Doring

Abstract

The covalent bonding of proteins to soluble polymers is closely related chemically to immobilization. Reactions similar to the activation of polymers are used. Polymers with a chemical structure similar to those used for solid phases and surfaces (gels, membranes, coatings) may be used. The disadvantage of using soluble polymers instead of insoluble compounds is the more laborious purification needed after polymer activation and reaction with the protein. The excessive reagent and unreacted protein have to be separated by precipitation (often with organic solvents), gel filtration, ultrafiltration or dialysis.

Keywords

Soluble Polymer DEAE Dextran Borax Buffer Laborious Purification Cytidine Monophosphate 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    WYKES, I.R., DUNNILL, P. & LILLY, M.D., Biochem. Biophys. Acta 250: 522, 1971.CrossRefGoogle Scholar
  2. 2.
    EPTON, R., MARR, G. & MORGAN, G.J., British Patent Application (Koch-Light ), 1976.Google Scholar
  3. 3.
    VON SPECHT, B.U., WAHL, M., KOLB, H.J. & BRENDEL, W., Aich. Int. Pharmacodyn. Ther. 213: 242, 1975.Google Scholar
  4. 4.
    ABUCHOWSKI, A., MCCOY, I.R., PALCZUK, N.C., VAN ES, T. & DAVIS, F.F., J. Biol. Chem. 252: 3582, 1977.Google Scholar
  5. 5.
    ABUCHOWSKI, A., VAN ES, T., PALCZUK, N.C. & DAVIS, F.F., J. Biol. Chem. 252: 3578, 1977.Google Scholar
  6. 6.
    VEGARND, G. & CHRISTENSEN, T.B., Biotechnol. Bioeng. 17: 1391, 1975.CrossRefGoogle Scholar
  7. 7.
    AXEN, R., MYRIN, P.A. & JANSON, J.C., Biopolymerz 9: 401, 1970.CrossRefGoogle Scholar
  8. 8.
    O’NEILL, S.P., WYKES, I.R., DUNNILL, P. & LILLY, M.D., Biotechnol. Bioeng. 13: 319, 1971.Google Scholar
  9. 9.
    VON SPECHT, B.-U., SEINFELD, H. & BRENDEL, W., Hoppe Seylers’s Z. Physiol. Chem. 354: 1659, 1973.Google Scholar
  10. 10.
    MARSHALL, J.J. & RABINOWITZ, M.L., J. Biol. Chem. 251: 1081, 1976.Google Scholar
  11. 11.
    DICKINSON, R.G. & JACOBSEN, N.W., Chem. Comm. 1799: 1719, 1970.Google Scholar
  12. 12.
    SCOTT, J.R., TROY, A. & MELVIN, E.H., Anal. Chem. 25: 1655, 1953.Google Scholar
  13. 13.
    CROOK, E.M., MATHIAS, A.P. & RABIN, B.R., Biochem. J. 74: 234, 1960.Google Scholar
  14. 14.
    RICK, W., in “Methoden der enzymatischen Analyse I,” (H.U. Bergmeyer, ed.) Verlag Chemie, Weinheim, 1970, p. 989.Google Scholar
  15. 15.
    BERGMEYER, H.U., GAWEHN, K. & BRASSL, M., in “Methoden der enzymatischen Analyse I,” (H.U. Bergmeyer, ed.) Verlag Chemie, Weinheim, 1970, p. 476.Google Scholar
  16. 16.
    Boehringer Mannheim GmbH, Biochemica Intormation 1: 121, 1973.Google Scholar
  17. 17.
    FOLK, J.E. & SCHIRMER, E.W., J. Biol. Chem. 238: 3884, 1963.Google Scholar
  18. 18.
    BERGMEYER, H.U., GAWEHN, K. & GRASSL, M., in “Methoden der enzymatischen Analyse I,” (H.U. Bergmeyer, ed.) Verlag Chemie, Weinheim, 1970, p. 416.Google Scholar

Copyright information

© Plenum Press, New York 1978

Authors and Affiliations

  • Roland R. Reiner
    • 1
  • Helga Doring
    • 1
  1. 1.Battelle-Institut e.V.Frankfurt am MainFederal Republic of Germany

Personalised recommendations