Antihelminthic effect of thymoquinone against biliary amphistome, Gigantocotyle explanatum

Farhat, Faiza; Wasim, Sobia; Abidi, S.M.A.

doi:10.1016/j.exppara.2022.108421

Cited by 4 publications

(1 citation statement)

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“…In order to deal with the enzyme, some of its hitherto unreported characteristics have also been investigated. The tegument of these parasites is a metabolically active surface, and since GeGGT is a tegumental enzyme, it may be a potential alternative pharmaceutical target (Farhat et al, 2022) in view of the increased need for alternative anthelmintic drugs or vaccine targets, as the majority of the chosen soluble proteins failed to demonstrate appreciable e cacy in eld tests for the development of vaccines against these parasitic helminths.…”

Section: Discussionmentioning

confidence: 99%

Affinity Purification, Identification and Biochemical Characterization of Gamma-Glutamyl Transpeptidase, a Membrane Anchored Enzyme of Gigantocotyle Explanatum

Faiza

Wasim²,

Rehman

et al. 2022

SSRN Journal

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Section: Discussionmentioning

confidence: 99%

Affinity Purification, Identification and Biochemical Characterization of Gamma-Glutamyl Transpeptidase, a Membrane Anchored Enzyme of Gigantocotyle Explanatum

Faiza

Wasim²,

Rehman

et al. 2022

SSRN Journal

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Affinity purification, identification, and biochemical characterization of Gamma-glutamyl transpeptidase, a membrane anchored enzyme of Gigantocotyle explanatum

et al. 2023

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Gamma-glutamyl Transpeptidase is an enzyme that facilitates the transfer of glutamyl groups from glutamyl peptides to other peptides or water. Additionally, it also participates in important processes such amino acid transport, cellular redox control, drug detoxi cation, apoptosis, and DNA fragmentation in a various organism. In the present study, GGT activity in Gigantocotyle explanatum was examined in order to characterize the enzyme in the helminth system. GGT is isolated using membrane solubilization and puri ed through a nity column chromatography (Con-A Sepharose column). Km and Vmax values, as well as the optimal pH, optimal temperature, and incubation period, are also determined using enzyme kinetics. The hetero-dimeric property of the enzyme is demonstrated by the puri ed GGT, which yielded two subunits of 65.5 and 55 kDa. The optimal pH and temperature are found to be 8.0 and 37°C, respectively. While assessing the optimal incubation time of the enzyme, it was observed that the puri ed GGT not only retained its functional integrity up to 15 min but also re ected considerable thermostability at higher temperatures, by retaining 78% and 25% of its initial activities at 50°C and 60°C, respectively. 1 mM concentration of 6-Diazo-5-Oxo Nor-isoleucine (DON), a speci c inhibitor of GGT, completely abolished GGT activity. These results suggest that GGT in these worms is a catalytically active enzyme with distinguishing characteristics that can be used for further study to comprehend its function in amphistome biology and in host-parasite relationships, especially since the potential therapeutic candidacy of the GGT enzyme has already been indicated in these groups of organisms.

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AlSagri,

Farhat,

Sohail

et al. 2024

J Acad Ethics

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Antihelminthic effect of thymoquinone against biliary amphistome, Gigantocotyle explanatum

Cited by 4 publications

References 65 publications

Affinity Purification, Identification and Biochemical Characterization of Gamma-Glutamyl Transpeptidase, a Membrane Anchored Enzyme of Gigantocotyle Explanatum

Affinity Purification, Identification and Biochemical Characterization of Gamma-Glutamyl Transpeptidase, a Membrane Anchored Enzyme of Gigantocotyle Explanatum

Affinity purification, identification, and biochemical characterization of Gamma-glutamyl transpeptidase, a membrane anchored enzyme of Gigantocotyle explanatum

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