Isolation and characterization of catalase isoforms from the mango stone weevil, Sternochetus mangiferae
| Autor: | Vivek Kempraj, Arthikirubha Ayyasamy, Kamala Jayanthi Pagadala Damodaram, Ravindra M. Aurade |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Reactive oxygen species 030102 biochemistry & molecular biology biology Host (biology) Weevil Aspergillus flavus biology.organism_classification Isozyme Sternochetus mangiferae 03 medical and health sciences 030104 developmental biology Enzyme chemistry Biochemistry Catalase Insect Science biology.protein |
| Zdroj: | Journal of Asia-Pacific Entomology. 19:239-245 |
| ISSN: | 1226-8615 |
| DOI: | 10.1016/j.aspen.2016.01.007 |
| Popis: | Insects use an arsenal of strategies to defend themselves against reactive oxygen species (ROS). An important strategy that is deemed vital for insects is their antioxidative enzyme systems. Among the many antioxidative enzyme systems, catalase plays a crucial role in protecting the host against ROS damage. However, studies on the biochemistry and characterization of insect catalases are meager. Recently, we discovered the presence of 2 isozymes of catalase in the mango stone weevil, Sternochetus mangiferae and one of the isozymes was inhibited by the weevil's entomopathogen, Aspergillus flavus. Therefore, in this study, we isolated, purified and characterized both isozymes to understand their biochemical functions. These two enzymes were purified to ~ 39 (CAT I) and ~ 31 (CAT II) folds and were subjected to de novo sequencing. Protein-BLAST results matched CAT I sequence to a general catalase from Drosophila and that of CAT II to an immune-regulated catalase of Drosophila. We found that Km and Vmax of CAT I was 4.077 ± 0.48 mM and 162.6 ± 6.80 U/mg, and that of CAT II was 3.767 ± 0.48 mM and 127.6 ± 5.561 U/mg, respectively. |
| Databáze: | OpenAIRE |
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