BMB Reports

Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
권호 표지

Recombinant Interferon-${\alpha}$ Cross-linked with Thymosin ${\alpha}$1 is Biologically Active

  • Received : 1996.03.25
  • Published : 1996.07.31
Download PDF
⟨ Previous Next ⟩

Abstract

Partially reduced interferon-a ($IFN-{\alpha}$) was cross-linked with thymosin ${\alpha}1$ ($T{\alpha}1$) using sulfo-succinimidyl (4-iodoacetyl) amino benzoate (SIAB), a bifunctional cross-linking reagent. The partially reduced $IFN-{\alpha}$ optimal for the cross-linking reaction was obtained by incubating native $IFN-{\alpha}$ with 0.5 mM DTT at $30^{\circ}C$ for 60~100 min. $T{\alpha}1$ was activated by incubating with sulfo-SIAB at $37^{\circ}C$ for 30 min to produce $T{\alpha}1-IAB$. The $T{\alpha}1-IFN-{\alpha}$ cross-linking was achieved by the reaction of the partially reduced $IFN-{\alpha}$ with $T{\alpha}1-IAB$. This cross-linking was between the sulfhydryl group of Cys1 in $IFN-{\alpha}$ and the N-terminal amino group of $T{\alpha}1$ through acetyl amino benzoate as a spacer. The immunological activity of the cross-linked molecule showed the same extent as that of $T{\alpha}1$, and most of the antiviral activity was retained compared to that of the partially reduced $IFN-{\alpha}$.

Keywords

References

  1. Nature v.284 ？Aguet, M. https://doi.org/10.1038/284459a0
  2. J. Biochem. Mol. Biol. (formly Korean Biochem. J.) v.28 Bae, T.;Chang, H.;Kim, J. H.;Park, S.J.
  3. Clin. Immunol. Im？munopathol. v.16 Dabrowski, M.P.;Dabrowska-Bernstein, B.K.;Brzosco, W.J.;Baniuch, L.;Kassur, B. https://doi.org/10.1016/0090-1229(80)90135-X
  4. Methods Enzymol. v.119 DeChiara, T.M.
  5. Int. J. Immunopharmacol. v.11 Favalli, C.;Mastino, A.;Jezzi, T. https://doi.org/10.1016/0192-0561(89)90172-0
  6. Cancer Immunol. Immunother. v.32 Garaci, E.;Mastino, A.;Pica, F.;Favalli, C. https://doi.org/10.1007/BF01771450
  7. Int. J. Clin. Lab. Res. v.24 Garaci, E.;Rocchi, G.;Perroni, L.;D'Agostini, C.;Soscia, F.;Grelli, S.;Mastino, A.;Favalli, C. https://doi.org/10.1007/BF02592405
  8. Proc. Natl. Acad. Sci. USA v.74 Goldstein, A.L.;Low, T.L.K.;McAdoo, M.;McClure, J.;Thurman, G.B.;Rossio, J.;Lai, C.Y.;Chang, D.;Wang, S.S.;Harvey, C.;Ramel, A.H.;Meienhofer, J. https://doi.org/10.1073/pnas.74.2.725
  9. Acta Oncologica v.28 Gresser, I. https://doi.org/10.3109/02841868909111205
  10. Proc. R. Soc. London Ser. B. v.147 Isaacs, A.;Lindenmann, J. https://doi.org/10.1098/rspb.1957.0048
  11. Korean J. BRM v.2 Kim, S.H.;Park, S.J.
  12. Immunopharmacology v.16 Kouttab, N.M. https://doi.org/10.1016/0162-3109(88)90018-5
  13. J. Biol. Chem. v.254 Low, T.L.K.;Goldstein, A.L.
  14. Ann. N.Y. Acad. Sci. v.332 Low, T.L.K.;Thurman, G.B.;Chincarini, C.;McClure, J.;Marshall, G.D.;Hu, S.K.;Goldstein, A.L. https://doi.org/10.1111/j.1749-6632.1979.tb47095.x
  15. J. Biol. Chem. v.254 Low, T.L.K.;Thurman, G.B.;McAdoo, M.;McClure, J.;Rossio, J.L.;Naylor, P.H.;Goldstein, A.L.
  16. Int. ？J. Immunopathol. Pharmacol. v.5 Mastino, A.;Favalli, C.;Grelli, S.;Garaci, E. https://doi.org/10.1177/039463209200500202
  17. Eur. J. Biochem. v.134 Mogensen, K.E.;Bandu, M.T. https://doi.org/10.1111/j.1432-1033.1983.tb07575.x
  18. Hepatology v.14 Mutchnick, M.G.;Appelman, H.D.;Chung, H.T.;Aragona, E.;Gupta, T.P.;Cummings, G.D.;Waggoner, J.G.;Hoofnagle, J.H.;Shafritz, D.A. https://doi.org/10.1002/hep.1840140302
  19. Current Concepts in Human Immunology Schulof. R.S.;Serrou, B.(ed.)
  20. Thymic Hormones and Lymphokines 83 Sheng, G.;Goldstein, A.L.(ed.)
  21. Eur. J. Immunol. v.12 Svedersky, L.P.;Hui, A.;May, L. https://doi.org/10.1002/eji.1830120314
  22. Springer Semin Immunopathol. v.9 Sztein, M.B.;Goldstein, A.L.
  23. Int. J. Immunopharmacol. v.11 Sztein, M.B.;Serrate, S.A https://doi.org/10.1016/0192-0561(89)90133-1
  24. J. Biol. Response Mod. v.3 Thurman, G.B.;Seals, C.;Low, T.L.K.
  25. J. Cell. Biochem., Suppl. v.6 Wetzel, R.
  26. Biochemical Actions of Hormones White, A.;Litwack, G.(ed.)
  27. Gerontology v.31 Zatz, M.M.;Goldstein, A.L. https://doi.org/10.1159/000212709