Skip to main content
Log in

A Low Molecular Weight Isoform of Hyaluronidase: Purification from Indian Cobra (Naja naja) Venom and Partial Characterization

  • Published:
Biochemistry (Moscow) Aims and scope Submit manuscript

Abstract

A low molecular weight isoform of hyaluronidase (NNH2) has been isolated from Indian cobra (Naja naja) venom by successive chromatography on Sephadex G-75 and CM-Sephadex C-25 columns. The apparent molecular weight determined by SDS-PAGE is 52 kD, and the pI value is 9.7. NNH2 is an endoglycosidase and exhibits in vitro absolute specificity for hyaluronan; it also hydrolyzed hyaluronan in human skin sections. NNH2 is nontoxic, but it indirectly potentiates the hemorrhagic activity of hemorrhagic complex-I. Curcumin, indomethacin, and tannic acid inhibited dose dependently the degradation of hyaluronan by NNH2.

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. Warrell, D. A. (1996) in Textbook of Medicine (Wealtherall, D. J., Ledingham, J. G. G., and Warrell, D. A., eds.) Oxford University Press, Oxford.

    Google Scholar 

  2. Chippaux, J. P. (1998) Bull. WHO, 76, 515–524.

    Google Scholar 

  3. Kini, R. M. (1997) Venom Phospholipase A 2 Enzymes: Structure, Function and Mechanism, J. Wiley, New York.

    Google Scholar 

  4. Kini, R. M. (1998) Toxicon, 36, 1659–1670.

    Google Scholar 

  5. Harvey, A. L., Bradley, K. N., Cocharan, S. A., Rowan, E. G., Pratt, J. A., Quillfeldt, J. A., and Jerusalinsky, D. A. (1998) Toxicon, 36, 1635–1640.

    Google Scholar 

  6. Markland, F. S. (1998) Toxicon, 36, 1749–1800.

    Google Scholar 

  7. Shashidhara murthy, R., Jagadeesha, D. K., Girish, K. S., and Kemparaju, K. (2002) Mol. Cell. Biochem., 229, 93–101.

    Google Scholar 

  8. Gutierrez, J. M., and Ownby, C. L. (2003) Toxicon, 42, 915–931.

    Google Scholar 

  9. Teixeira, C. F. P., Landucci, E. C. T., Antunes, E., Chacur, M., and Cury, Y. (2003) Toxicon, 42, 947–962.

    Google Scholar 

  10. Gopalakrishnakone, P., Ponraj, D., and Thwin, M. M. (1997) in Venom Phospholipase A 2 Enzymes: Structure, Function and Mechanism (Kini, R. M., ed.) John Wiley & Sons Ltd., pp. 287–319.

  11. Gutierrez, J. M., and Rucavado, A. (2000) Biochimie, 82, 841–850.

    Google Scholar 

  12. Girish, K. S., Jagadeesha, D. K., Rajeev, K. B., and Kemparaju, K. (2002) Mol. Cell. Biochem., 40, 105–110.

    Google Scholar 

  13. Anai, K., Sugiki, M., Yoshida, E., and Maruyama, M. (2002) Toxicon, 40, 63–68.

    Google Scholar 

  14. Girish, K. S., Shashidhara murthy, R., Nagaraju, S., Gowda, T. V., and Kemparaju, K. (2004) Biochimie, 86, 193–202.

    Google Scholar 

  15. Maruyama, M., Sugiki, M., Yoshida, E., Mihara, H., and Nakajima, N. (1992) Toxicon, 30, 853–864.

    Google Scholar 

  16. Estevao-Costa, M. I., Diniz, C. R., Magalhaes, A., Markland, F. S., and Sanchez, E. F. (2000) Thromb. Res., 99, 363–376.

    Google Scholar 

  17. Leon, G., Valverde, J. M., Rojas, G., Lomonte, B., and Gutierrez, J. M. (2000) Toxicon, 38, 233–244.

    Google Scholar 

  18. Yingprasertchai, S., Bunyasrisawt, S., and Ratanabanangkoon, K. (2003) Toxicon, 42, 635–646.

    Google Scholar 

  19. Tu, A. T., and Hendon, R. R. (1983) Comp. Biochem. Physiol., 76, 337–383.

    Google Scholar 

  20. Stern, M., and Stern, R. (1992) Matrix, 12, 397–403.

    Google Scholar 

  21. Laemmli, U. K. (1970) Nature, 227, 680–685.

    Google Scholar 

  22. Fiszer-szafarz, B. (1984) Analyt. Biochem., 143, 76–81.

    Google Scholar 

  23. Cevellos, M. A., Navarro-Duque, C., Varela-Julia, M., and Alagon, A. C. (1992) Toxicon, 30, 925–930.

    Google Scholar 

  24. Menzel, E. J., and Farr, C. (1998) Cancer Lett., 131, 3–11.

    Google Scholar 

  25. Uma, B. (1999) Ph. D. Thesis, University of Mysore, Mysore, India.

  26. Kondo, H., Kondo, S., Ikezawa, H., Muruta, R., and Ohsaka, A. (1960) Jpn. J. Med. Sci. Biol., 13, 43–51.

    Google Scholar 

  27. Tammi, R., Ripellino, J. A., Margolis, R. U., and Tammi, M. (1988) J. Invest. Dermatol., 90, 412–414.

    Google Scholar 

  28. Meyer, L. J. M., and Stern, R. (1994) J. Invest. Dermatol., 102, 385–389.

    Google Scholar 

  29. Rucavado, A., Escalante, T., Franceschi, A., Chaves, F., Leon, G., Cury, Y., Ovadia, M., and Gutierrez, J. M. (2000) Am. J. Trop. Med. Hyg., 63, 313–319.

    Google Scholar 

  30. Escalante, T., Franceschi, A., Rucavado, A., and Gutierrez, J. M. (2000) Biochem. Pharmacol., 60, 269–274.

    Google Scholar 

  31. Leon, G., Rojas, G., Lomonte, B., and Gutierrez, J. M. (1997) Toxicon, 35, 1627–1637.

    Google Scholar 

  32. Gutierrez, J. M., Chaves, F., Rojas, G., Bogarin, G., and Lomonte, B. (1996) in Envenomings and Their Treatments (Bon, C., and Goyffon, M., eds.) Foundation Marcel Merieux Luyon, Marcel, pp. 223–231.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to K. Kemparaju.

Additional information

__________

Translated from Biokhimiya, Vol. 70, No. 6, 2005, pp. 855–860.

Original Russian Text Copyright © 2005 by Girish,, Kemparaju.

Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM04-224, October 24, 2004.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Girish, K.S., Kemparaju, K. A Low Molecular Weight Isoform of Hyaluronidase: Purification from Indian Cobra (Naja naja) Venom and Partial Characterization. Biochemistry (Moscow) 70, 708–712 (2005). https://doi.org/10.1007/s10541-005-0172-6

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10541-005-0172-6

Key words

Navigation