Skip to main content
Log in

Purification and properties of serine proteinases from European catfish Silurus glanis L. pancreas

  • Published:
Applied Biochemistry and Microbiology Aims and scope Submit manuscript

Abstract

Three trypsin isoforms (designated as T1, T2, and T3), three chymotrypsin isoforms (Kh1, Kh2, and Kh3), and two elastase isoforms (E1 and E2) were isolated from the pancreas of European catfish Silurus glanis L. by salting out with (NH4)2SO4, gel chromatography on Sephadex G-75, and ion exchange chromatography on DEAE cellulose. Isoelectric points of the enzymes, determined by isoelectric focusing, amounted to 4.42 for T1, 5.64 for T2, 6.90 for T3, 4.93 for Kh1, 5.23 for Kh2, 6.18 for Kh3, 6.17 for E1, and 8.48 for E2. Molecular weights of proteinases within each group were close and amounted to 30,100 Da for trypsins, 39,800 Da for chymotrypsins, and 24,000 Da for elastases. The enzymes isolated displayed maximal activities at alkaline pH values. Inhibitor analysis demonstrated that all the proteinases isolated from European catfish pancreas belonged to the serine type.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

REFERENCES

  1. Zhuravskaya, N.K. and Izotov, O.V., Myasnaya Industriya, 2002, no. 9, pp. 23–26.

  2. Snitsar’, A., Chernukha, I., and Al’murziev, M., Mezhdunar. Agroprom. Zh., 1989, no. 6, pp. 118–121.

  3. Glik, B. and Pasternak, Dzh., Molekulyarnaya biotekhnologiya: printsipy i primenenie (Molecular Biotechnology: Foundations and Use), Moscow: Mir, 2002.

    Google Scholar 

  4. Belen’kii, N.G., Polonskaya, L.B., and Chamin, N.N., Novoe v proizvodstve fermentov i fermentativnykh preparatov iz zhivotnogo syr’ya (Advances in Production of Enzymes and Enzymatic Preparations from Animal Raw Materials), Moscow: TsINTI Pishcheprom, 1966.

    Google Scholar 

  5. Mosolov, V.V., Proteoliticheskie Fermenty (Proteolytic Enzymes), Moscow: Nauka, 1971.

    Google Scholar 

  6. Kleine, R., Biologische Rundschau, 1969, no. 7, pp. 159–169.

  7. Yakovenko, E.P., Klinich. Farm. Ter., 1998, no. 1, pp. 17–20.

  8. Berezov, T.T., Sorosovskii Obrazovatel’nyi Zh., 1996, no. 3, pp. 23–27.

  9. Borovskii, E.V., Klinicheskaya endodontiya (Clinical Root Canal Treatment), Moscow: AO Stomatologiya, 2003.

    Google Scholar 

  10. Kuznetsova, T.A., Markova, E.A., and Gonchar, A.I., Vestn. Ros. Ass. Akush.-Ginekol., 1997, no. 1, pp. 81–83.

  11. Yoshinaka, R., Sato, M., Sato, T., and Ikeda, S., Comp. Biochem. Physiol., 1984, vol. 78B, no.3, pp. 569–573.

    CAS  Google Scholar 

  12. Simpson, B.K. and Haard, N.F., Comp. Biochem. Physiol., 1985, vol. 80B, no.3, pp. 475–480.

    CAS  Google Scholar 

  13. Khablyuk, V.V. and Proskuryakov, M.T., Prikl. Biokhim. Mikrobiol., 1983, vol. 19, no.3, pp. 403–407.

    CAS  Google Scholar 

  14. Tuppy, H., Wiesbauer, U., and Wintersberger, E., Hoppe Seylers Z. Physiol. Chem., 1962, vol. 329, nos.3–6, pp. 278–288.

    Google Scholar 

  15. Erlanger, B.F., Edel, F., and Cooper, A.G., Arch. Biochem. Biophys., 1966, vol. 115, pp. 206–210.

    Article  CAS  PubMed  Google Scholar 

  16. Katagiri, K., Takeuchi, T., Taniguchi, K., and Sasaki, M., Anal. Biochem., 1978, vol. 86, pp. 159–165.

    CAS  PubMed  Google Scholar 

  17. Northrop, J.H., Kunitz, M., and Herriot, R.M., Crystalline Enzyme, New York: Columbia Univ., 1948.

    Google Scholar 

  18. Grant, N.H. and Robbins, K.C., Arch. Biochem. Biophys., 1957, vol. 66, pp. 396–403.

    CAS  PubMed  Google Scholar 

  19. Pyatnitskii, N.P. and Selyukova, M.N., Vopr. Pitan., 1960, no. 2, pp. 42–48.

  20. Righetti, P., Isoelectric Focusing. Theory, Methodology and Applications, Amsterdam: Elsevier, 1983. Translated under the title Izoelektricheskoe fokusirovanie: teoriya, metody i primenenie, Moscow: Mir, 1986.

    Google Scholar 

  21. Reeck, G.R., Winter, W.R., and Neurath, H., Biochemistry, 1970, vol. 9, no.6, pp. 1399–1403.

    Google Scholar 

  22. Ardelt, W., Biochim. Biophys. Acta, 1974, vol. 341, pp. 318–326.

    CAS  PubMed  Google Scholar 

  23. Allan, B.J., Zagen, N.I., and Keller, P.J., Arch. Biochem. Biophys., 1970, vol. 136, pp. 529–540.

    CAS  PubMed  Google Scholar 

  24. Asgeirsson, B. and Bjarnason, B., Comp. Biochem. Physiol., 1991, vol. 99B, pp. 327–335.

    CAS  Google Scholar 

  25. Kitamikado, M. and Tachino, S., Bull. Jpn. Soc. Sci. Fish., 1960, vol. 26, pp. 685–690.

    CAS  Google Scholar 

  26. Munilla-Moran, R. and Saborido-Rey, F., Comp. Biochem. Physiol., 1996, vol. 113B, pp. 818–826.

    Google Scholar 

  27. Yoshinaka, R., Sato, M., Suzuki, T., and Ikeda, S., Comp. Biochem. Physiol., 1984, vol. 77B, no.1, pp. 1–6.

    CAS  Google Scholar 

  28. Walsh, K.A., Metods Enzymol., New York: Academic, 1970, vol. 19, pp. 41–63.

    Google Scholar 

  29. Wilcox, P.E., Metods Enzymol., New York: Academic, 1970, vol. 19, pp. 64–108.

    Google Scholar 

  30. Smillie, L., Furka, A., Nagabhushan, N., and Stevenson, K., Nature, 1968, vol. 218, no.5139, pp. 343–346.

    CAS  PubMed  Google Scholar 

  31. Colomb, E., Guy, O., Deprex, P., Michel, P., and Figarella, C., Biochim. Biophys. Acta, 1979, vol. 525, no.1, pp. 186–193.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

Translated from Prikladnaya Biokhimiya i Mikrobiologiya, Vol. 41, No. 2, 2005, pp. 158–164.

Original Russian Text Copyright © 2005 by Ulitina, Khablyuk, Proskuryakov.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Ulitina, N.N., Khablyuk, V.V. & Proskuryakov, M.T. Purification and properties of serine proteinases from European catfish Silurus glanis L. pancreas. Appl Biochem Microbiol 41, 139–144 (2005). https://doi.org/10.1007/s10438-005-0023-7

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10438-005-0023-7

Keywords

Navigation