, Volume 39, Issue 10, pp 1109–1111 | Cite as

Induction of proteolytic activity in serum by treatment with anionic detergents and organic solvents

  • D. Berger
  • T. L. Vischer
  • A. Micheli
Short Communications Biochemistry


Using casein plates as a sensitive assay for proteolytic activity, it was observed that sodium-dodecyl sulfate (SDS) and other anionic detergents induce caseinolysis when mixed with sera and plasma. Caseinolysis was dependent on the presence of plasminogen in the fluids and could be blocked by inhibitors of serine proteases and antibody to plasminogen. Similarly, organic solvents such as isopropanol induced caseinolysis after mixing with plasma, but not normal serum. Isopropanol dissociated complexes ofa1-antitrypsin ora2-macroglobulin with trypsin preformed in vitro. As both SDS and organic solvents are widely used in biochemical investigations of biological fluids, attention should be paid to the possible induction of proteolysis.


Sulfate Serine Trypsin Organic Solvent Isopropanol 
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. 3.
    Bjerrum, O.J., Ramlau, J., Clemmensen, I., Ingild, A., and Bog-Hansen, T.C., Scand. J. Immun.4 (1975), suppl. 2, 81.Google Scholar
  2. 4.
    Vischer, T.L., and Berger, D., J. reticuloendoth. Soc.28 (1980) 427.Google Scholar
  3. 5.
    Pannell, R., Johnson, D., and Travis, J., Biochemistry13 (1974) 5439.Google Scholar
  4. 6.
    Fahey, J.L., and Terry, E.W., in: Handbook of experimental immunology, vol. 1, 2nd edn, p. 7.1. Ed. D.M. Weir. Blackwell, Oxford/London/Edinburg/Melbourne 1973.Google Scholar
  5. 7.
    Radcliffe, R., and Heinze, T., Archs Biochem. Biophys.189 (1978) 185.Google Scholar
  6. 8.
    Ogston, D., Ogston, C.M., Ratnoff, O.D., and Forbes, C.D., J. clin. Invest.48 (1969) 1786.Google Scholar
  7. 9.
    Goldsmith, G.H., Saito, K., and Ratnoff, O.D., J. clin. Invest.62 (1978) 54.Google Scholar
  8. 10.
    Alkjaersig, N., Fletcher, A.P., and Sherry, S., J. biol. Chem.233 (1958) 81.Google Scholar
  9. 11.
    Lijnen, H.R., and Collen, D., Semin. Thromb. Hemostasis8 (1982) 2.Google Scholar
  10. 12.
    Violand, B.N., Byrne, R., and Castellino, F.J., J. biol. Chem.253 (1978) 5395.Google Scholar
  11. 13.
    Kluft, C., J. Lab. clin. Med.91 (1978) 83.Google Scholar
  12. 14.
    Katsuda, K., and Maeno, H., Thromb. Res.19 (1980) 655.Google Scholar
  13. 15.
    Hadding, U., Dierich, M., Koenig, W., and Limbert, M., Eur. J. Immun.3 (1973) 527.Google Scholar
  14. 16.
    Loos, M., and Bitter-Suermann, D., Immunology31 (1976) 931.Google Scholar
  15. 17.
    Carlin, G., and Bang, N.U., Thromb. Res.19 (1980) 535.Google Scholar
  16. 18.
    Weber, K., Pringle, J.R., and Osborn, M., Meth. Enzym.26 (1972) 3.Google Scholar
  17. 19.
    Diamantstein, T., Vogt, W., Ruehl, H., and Bochert, G., Eur. J. Immun.3 (1973) 488.Google Scholar
  18. 20.
    Vischer, T.L., Agents Actions6 (1976) 479.Google Scholar
  19. 21.
    Vischer, T.L., J. Immun.113 (1974) 58.Google Scholar
  20. 22.
    Kaplan, J.G., and Bona, C., Exp. Cell Res.88 (1974) 388.Google Scholar
  21. 23.
    Vischer, T.L., Bretz, U., and Baggiolini, M., J. exp. Med.144 (1976) 863.Google Scholar
  22. 24.
    Kast, R.E., Oncology29 (1974) 249.Google Scholar
  23. 25.
    Vitetta, E.S., and Uhr, J.W., Immun. Rev.37 (1977) 50.Google Scholar
  24. 26.
    Christensen, L.R., J. gen. Physiol.30 (1946) 149.Google Scholar
  25. 27.
    Gordon, E.M., Ratnoff, O.D., and Goldsmith, H.G., J. Lab. clin. Med.95 (1980) 507.Google Scholar

Copyright information

© Birkhäuser Verlag 1983

Authors and Affiliations

  • D. Berger
    • 1
  • T. L. Vischer
    • 1
  • A. Micheli
    • 1
  1. 1.Division of RheumatologyHôpital cantonal universitaireGenève 4(Switzerland)

Personalised recommendations