Preliminary study on isolation, purification and partial characterization of phospholipase A2 from a Nigerian Naja nigricolis venom

Authors

  • Yahaya Tijani Department of Biochemistry Faculty of Life Sciences University of Maiduguri
  • Muhammad Ibrahim Khala Department of Biochemistry, Faculty of Life Sciences, University of Maiduguri, Borno State, Nigeria. PMB 1069
  • Miriam Watafua Heriot-Watt University, Edinburgh, Unite Kingdom
  • Afiniki Bitrus Mbya Department of Biochemistry, Faculty of Life Sciences, University of Maiduguri, Borno State, Nigeria. PMB 1069
  • Abubakar Shettima Department of Microbiology, Faculty of Life Sciences, University of Maiduguri, Borno State, Nigeria
  • Mohammed Abba Dige Department of Biotechnology, Faculty of Life Sciences, University of Maiduguri, Borno State, Nigeria
  • Andrew Onu Department of Biochemistry, Faculty of Chemical and Life Sciences, Usman Danfodiyo university Sokoto, Nigeria.
  • Hassan Mohammed Khala Department of Biochemistry, Faculty of Life Sciences, University of Maiduguri, Borno State, Nigeria. PMB 1069
  • Bulama Burah Department of Biochemistry, Faculty of Life Sciences, University of Maiduguri, Borno State, Nigeria. PMB 1069
  • Tan Choo Hock Venom Research and Toxicology Laboratory, Department of Pharmacology, Faculty of Medicine, University of Malaya, Kaula Lumpur, Malaysia
  • Hassan Zanna Department of Biochemistry, Faculty of Life Sciences, University of Maiduguri, Borno State, Nigeria. PMB 1069

DOI:

https://doi.org/10.54117/

Keywords:

Naja nigricolis, Nigerian, isolation, Purification, Phospholipase A2

Abstract

Phospholipase A2 in Naja species of snake is an enzyme involved in venom toxicity. It hydrolyzes phospholipids, affecting cell membranes. Understanding its properties can contribute to venom research, offering insights into potential medical applications or antivenom development. In this study, isolation and purification of phospholipase A2 from Nigerian Naja nigricolis venom was achieved with the use of SDS-PAGE, Resource-S-Cation-Exchange Chromatography and Reverse-phase HPLC. The crude venom was also assessed for PLA2 optimum pH and temperature. A successful isolation and purification was achieved with a notable yield of 768 µg. The enzyme has a molecular weight of 13 kDa and exhibits optimal activity at a pH of 8.0 and a temperature of 500C. This purification method proves effective in isolating the enzyme, offering potential applications in research and furthering our understanding of the Nigerian Naja nigricolis venom phospholipase A2. These findings provide valuable insights into the characteristics of Naja nigricolis phospholipase A2 for potential applications in venomics and antivenomics.

Downloads

Published

2024-12-30

How to Cite

Preliminary study on isolation, purification and partial characterization of phospholipase A2 from a Nigerian Naja nigricolis venom. (2024). Journal of Current Biomedical Research, 4(6, November-December), 1906-1917. https://doi.org/10.54117/

Similar Articles

1-10 of 21

You may also start an advanced similarity search for this article.