Skip to main content
Log in

Purification and characterization of a novel phospholipase A2 from king cobra (Ophiophagus hannah) venom

  • Published:
Journal of Protein Chemistry Aims and scope Submit manuscript

Abstract

A novel phospholipase A2, designated as Oh-DE-2, was isolated from the venom ofOphiophagus hannah (king cobra) by successive chromatography on SP-Sephadex C-25, DE-52, and Q-Sepharose columns. Oh-DE-2 with pI 5.1 showed an apparent molecular weight of 14 kD as revealed by SDS-PAGE and gel filtration. The amino acid sequence was homologous with those of PLA2s from Elapidae venoms. Oh-DE-2 was effectively inactivated byp-bromophenacyl bromide, indicating that the conserved His-48 is essential for its enzymatic activity. However, modification of the conserved Trp-19 did not cause a precipitous drop in the enzymatic activity of Oh-DE-2 as observed with PLA2s fromNaja naja atra andBungarus multicinctus venoms. A quenching study showed that the microenvironment of Trp in Oh-DE-2 was inaccessible to acrylamide, iodide, or cesium, a finding which was different from those observed with PLA2s fromN. naja atra andB. multicinctus venoms. These results might suggest that, unlike other PLA2 enzymes, Trp-19 in Oh-DE-2 is not directly involved in its enzymatic mechanisms.

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

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Chiou, JY., Chang, LS., Chen, LN. et al. Purification and characterization of a novel phospholipase A2 from king cobra (Ophiophagus hannah) venom. J Protein Chem 14, 451–456 (1995). https://doi.org/10.1007/BF01888139

Download citation

  • Received:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01888139

Key words

Navigation