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

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.

Authors

Publication Details

Journal
Journal of Current Biomedical Research
Published
2024-12-11
DOI
https://doi.org/10.54117/jcbr.v4i6.4
Primary Topic
Venomous Animal Envenomation and Studies
Type
article
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article

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

Yahaya Tijani, Miriam Watafua, Muhammad Ibrahim Khala, Afiniki Bitrus Mbya
1 links
Journal of Current Biomedical Research
Venomous Animal Envenomation and Studies
article

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

Yahaya Tijani, Miriam Watafua, Muhammad Ibrahim Khala, Afiniki Bitrus Mbya
article en

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.

Journal of Current Biomedical ResearchVol. 4(6)
Openalex Percentile: Top 72%
Venomous Animal Envenomation and Studies
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