Proteomic And Biochemical Analysis Of Detoxification Enzyme In Musca Domestica L. (Diptera: Muscidae) And Its Response Upon Prolonged Exposure Of Insecticide

This study provides the proteomic and biochemical information of the detoxification enzymes namely acetylcholinesterase (AChE), α-esterase (α-est), β- esterase (β-est), glutathione s-transferase (GST) and cytochrome P450 (Cyt P450) in susceptible (adult, larvae and pupae) and poultry strains (lar...

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Main Author: Manoharan, Kalaavathi
Format: Thesis
Language:English
Published: 2024
Subjects:
Online Access:http://eprints.usm.my/62045/
http://eprints.usm.my/62045/1/KALAAVATHI%20AP%20MANOHARAN%20-%20TESIS24.pdf
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author Manoharan, Kalaavathi
author_facet Manoharan, Kalaavathi
author_sort Manoharan, Kalaavathi
building USM Institutional Repository
collection Online Access
description This study provides the proteomic and biochemical information of the detoxification enzymes namely acetylcholinesterase (AChE), α-esterase (α-est), β- esterase (β-est), glutathione s-transferase (GST) and cytochrome P450 (Cyt P450) in susceptible (adult, larvae and pupae) and poultry strains (larvae) Musca domestica. Upon whole protein analysis, number of proteins discovered in larvae was highest (441), followed by adults (181) and pupae (115) which concluded specific proteins are necessary for the proper progression of each developmental phase. Meanwhile, the enzyme activities as well as the protein content of the susceptible strain were found to have significantly varied enzymatic activity across the developmental stages (p<0.05). Thirthy four distinct peptides of the targeted detoxification enzyme were discovered at various developmental stages of the susceptible strain. Functional analysis of the targeted peptides of the susceptible strains exposed that in addition to their functions in detoxification, the multifunctional enzymes were also found to be developmental-related proteins that responsible in various biological process, molecular functions and KEGG pathways to complete metamorphosis. Overall, it has been observed that at the larvae stage, the targeted developmental related detoxification peptides were more expressed and were the most enriched in terms of biological process, molecular function and KEGG
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format Thesis
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institution Universiti Sains Malaysia
institution_category Local University
language English
last_indexed 2025-11-15T19:13:38Z
publishDate 2024
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spelling usm-620452025-03-24T03:20:45Z http://eprints.usm.my/62045/ Proteomic And Biochemical Analysis Of Detoxification Enzyme In Musca Domestica L. (Diptera: Muscidae) And Its Response Upon Prolonged Exposure Of Insecticide Manoharan, Kalaavathi QH1 Natural history (General - Including nature conservation, geographical distribution) This study provides the proteomic and biochemical information of the detoxification enzymes namely acetylcholinesterase (AChE), α-esterase (α-est), β- esterase (β-est), glutathione s-transferase (GST) and cytochrome P450 (Cyt P450) in susceptible (adult, larvae and pupae) and poultry strains (larvae) Musca domestica. Upon whole protein analysis, number of proteins discovered in larvae was highest (441), followed by adults (181) and pupae (115) which concluded specific proteins are necessary for the proper progression of each developmental phase. Meanwhile, the enzyme activities as well as the protein content of the susceptible strain were found to have significantly varied enzymatic activity across the developmental stages (p<0.05). Thirthy four distinct peptides of the targeted detoxification enzyme were discovered at various developmental stages of the susceptible strain. Functional analysis of the targeted peptides of the susceptible strains exposed that in addition to their functions in detoxification, the multifunctional enzymes were also found to be developmental-related proteins that responsible in various biological process, molecular functions and KEGG pathways to complete metamorphosis. Overall, it has been observed that at the larvae stage, the targeted developmental related detoxification peptides were more expressed and were the most enriched in terms of biological process, molecular function and KEGG 2024-02 Thesis NonPeerReviewed application/pdf en http://eprints.usm.my/62045/1/KALAAVATHI%20AP%20MANOHARAN%20-%20TESIS24.pdf Manoharan, Kalaavathi (2024) Proteomic And Biochemical Analysis Of Detoxification Enzyme In Musca Domestica L. (Diptera: Muscidae) And Its Response Upon Prolonged Exposure Of Insecticide. Masters thesis, Universiti Sains Malaysia.
spellingShingle QH1 Natural history (General - Including nature conservation, geographical distribution)
Manoharan, Kalaavathi
Proteomic And Biochemical Analysis Of Detoxification Enzyme In Musca Domestica L. (Diptera: Muscidae) And Its Response Upon Prolonged Exposure Of Insecticide
title Proteomic And Biochemical Analysis Of Detoxification Enzyme In Musca Domestica L. (Diptera: Muscidae) And Its Response Upon Prolonged Exposure Of Insecticide
title_full Proteomic And Biochemical Analysis Of Detoxification Enzyme In Musca Domestica L. (Diptera: Muscidae) And Its Response Upon Prolonged Exposure Of Insecticide
title_fullStr Proteomic And Biochemical Analysis Of Detoxification Enzyme In Musca Domestica L. (Diptera: Muscidae) And Its Response Upon Prolonged Exposure Of Insecticide
title_full_unstemmed Proteomic And Biochemical Analysis Of Detoxification Enzyme In Musca Domestica L. (Diptera: Muscidae) And Its Response Upon Prolonged Exposure Of Insecticide
title_short Proteomic And Biochemical Analysis Of Detoxification Enzyme In Musca Domestica L. (Diptera: Muscidae) And Its Response Upon Prolonged Exposure Of Insecticide
title_sort proteomic and biochemical analysis of detoxification enzyme in musca domestica l. (diptera: muscidae) and its response upon prolonged exposure of insecticide
topic QH1 Natural history (General - Including nature conservation, geographical distribution)
url http://eprints.usm.my/62045/
http://eprints.usm.my/62045/1/KALAAVATHI%20AP%20MANOHARAN%20-%20TESIS24.pdf