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Journal of Solid-Phase Biochemistry

, Volume 3, Issue 1, pp 49–56 | Cite as

Study on the properties of dextran-linked adenine nucleotide derivatives

  • Chi-yu Lee
Article
  • 19 Downloads

Abstract

A simple method is described for the preparation of dextran-linked coenzyme derivatives. Several different 8-(6-aminohexyl)amino-adenine nucleotide coenzymes and their derivatives were covalently attached to dextran by incubation with bromohydroxypropyl derivatives of dextran at room temperature in an alkaline medium. The polymer-linked adenine nucleotide derivatives were separated from the free coenzyme derivatives by a Sephadex G-50 column. The prepared dextran derivatives have ligand densities ranging from 20 to 100 μmol/g of dextran derivatives depending on the conditions of coupling and derivatives. NMR studies revealed that proton resonances of the polymer-linked coenzymes exhibit short transverse relaxation times (T2) but long longitudinal relaxation times (T1) This phenomenon was interpreted in terms of the anisotropic motions of the dextran-bound coenzyme derivatives in which the fast axial motions and slow restricted transverse motions of the bound coenzyme derivatives are postulated. These observations could properly explain why the polymer-linked coenzymes exhibit lower biological activity, but similar binding affinity to most enzymes.

Keywords

Dextran Proton Resonance Longitudinal Relaxation Time Ligand Density Anisotropic Motion 
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.

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References

  1. 1.
    Marconi, W. (1974) Industrial Aspects of Biochemistry, Vol. 3, Part 1,Spencer, B. (ed), North-Holland, Amsterdam, pp. 139–186.Google Scholar
  2. 2.
    Albertsson, P.-Å. (1971) Partition of Cell Particles and Macromolecules, 2nd ed.,Almquist andWiksell (eds.), Wiley, New York.Google Scholar
  3. 3.
    Shanbhag, V. P., andJohansson, G. (1974) Biochem. Biophys. Res. Commun. 61: 114.CrossRefGoogle Scholar
  4. 4.
    Flanagan, S. D., andBarondes, S. H. (1975) J. Biol. Chem. 250: 1484.Google Scholar
  5. 5.
    Wykes, J.R., Dunnill, P., andLilly, N.D. (1972) Biochem. Biophys. Acta 280: 260.Google Scholar
  6. 6.
    Larsson, P. O., andMosbach, K. (1974) FEBS Lett. 46: 119.CrossRefGoogle Scholar
  7. 7.
    Zappelli, P., Rossodivita, A., andRe, L. (1975). Eur. J. Biochem. 54: 475.CrossRefGoogle Scholar
  8. 8.
    Bachman, B., andLee, C.-Y. (1976) Anal. Biochem. 153–160.Google Scholar
  9. 9.
    Lee, C.-Y., Lappi, B. A., Wermuth, B., andEverse, J. (1974) Arch. Biochem. Biophys. 163:561.CrossRefGoogle Scholar
  10. 10.
    Lee, C.-Y., andKaplan, N. O. (1975) Arch. Biochem. Biophys. 168: 665.CrossRefGoogle Scholar
  11. 11.
    Lee, C.-Y., andKaplan, N. O. (1976) J. Macromol. Sci. Chem. A-10: 15.CrossRefGoogle Scholar
  12. 12.
    Lee, C.-Y., Lazarus, L. H., Kapakoff, D. S., Laver, M. B., Russell, P. J., andKaplan, N. O. (1977) Arch. Biochem. Biophys. 178: 8.CrossRefGoogle Scholar
  13. 13.
    Trayer, I. P., Trayer, H. R. Small, D. A. P., andBottomley, R. C. (1974) Biochem. J. 139:609.Google Scholar
  14. 14.
    Lee, C.-Y., andJohansson, C.-J. (1977) Anal. Biochem. 77:90.CrossRefGoogle Scholar
  15. 15.
    Pegoraro, B.,Yuan, J. H., andLee, C.-Y. (1978) Mol. Cell. Biochem., in press.Google Scholar
  16. 16.
    Lee, C.-Y.,Voss, H. F., andKaplan, N. O. (1975) Abstract presented at Pacific Conference on Chemistry and Spectroscopy.Google Scholar
  17. 17.
    Carrington, A., andMcLachlan, A. D. (1967) Introduction to Magnetic Resonance, Harper & Row, New York, Evanston, London.Google Scholar
  18. 18.
    Horwitz, A. F., Horsley, W. J., andKlein, M. P. (1972) Proc. Natl. Acad. Sci. U.S.A. 69: 590.CrossRefGoogle Scholar
  19. 19.
    Fuller, C. W., andBright, H. J. (1977) J. Biol. Chem. 252: 6631.Google Scholar
  20. 20.
    Muramatsu, M., Urabe, I., Yamada, Y., andOkada, H. (1977) Eur. J. Biochem. 80: 111.CrossRefGoogle Scholar
  21. 21.
    Voss, H. F., Lee, C.-Y., andKaplan, N. O. (1978) Enzyme Engineering, Vol. III,Pye, K. (ed.), Plenum Press, New York, in press.Google Scholar

Copyright information

© Humana Press Inc. 1978

Authors and Affiliations

  • Chi-yu Lee
    • 1
  1. 1.Laboratory of Environmental Mutagenesis National Institute of Environmental Health Sciences Research Triangle ParkNorth Carolina

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