Changes of peroxidase with age in drosophila

Armstrong, Donald; Rinehart, R. W.; Dixon, Linda; Reigh, Darryel L.

doi:10.1007/bf02432020

Cited by 39 publications

(6 citation statements)

References 22 publications

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“…Peroxidase activity was determined in microplate wells using a cocktail of 100 µL of 50 mM phosphate buffer (pH 7), 60 µL of guaiacol, 20 µL of enzyme extract, and 60 µL of a freshly prepared 0.1 M H2O2 [37]. A 96-well microplate reader was used to quantify the rise in absorbance induced by accelerated substrate oxidation in the presence of H2O2.…”

Section: Peroxidase Assaymentioning

confidence: 99%

Differential Activities of Antioxidant Enzymes, Superoxide Dismutase, Peroxidase, and Catalase vis-à-vis Phosphine Resistance in Field Populations of Lesser Grain Borer (Rhyzopertha dominica) from India

et al. 2023

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Susceptibility to phosphine was compared in 15 populations of lesser grain borer (Rhyzopertha dominica) collected from grain storage godowns across India. A high level of resistance to phosphine was noticed in R. dominica collected from northern India compared to those collected from northeastern regions of India. The median lethal concentration values varied from 0.024 mg/L to 1.991 mg/L, with 1.63 to 82.96-fold resistance compared to laboratory susceptible checks. Antioxidant enzymes have been reported to negate the reactive oxygen species generated upon encountering the fumigant phosphine. Distinct differences in the activity of antioxidant enzymes were noticed in the field populations exposed to phosphine. Peroxidase activity varied between 1.28 and 336.8 nmol H2O2 reduced/min/mg protein. The superoxide dismutase inhibition rate was between 81.29 and 99.66%, and catalase activity varied between 6.28 and 320.13 nmol H2O2 reduced/min/mg protein. The findings of our investigation show that the activities of peroxidase and superoxide dismutase are positively linked (p < 0.01) with an increase in resistance ratios, whereas catalase was found to have a negative association with resistance to phosphine. The reported results elucidate the differential activities of principal antioxidant enzymes in scavenging the oxyradicals (O2•−, H2O2, •OH) associated with tolerance to phosphine in R. dominica.

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Section: Peroxidase Assaymentioning

confidence: 99%

Differential Activities of Antioxidant Enzymes, Superoxide Dismutase, Peroxidase, and Catalase vis-à-vis Phosphine Resistance in Field Populations of Lesser Grain Borer (Rhyzopertha dominica) from India

et al. 2023

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“…In previous studies of aging in the housefly, Muscu dornesticu, it was assumed that this non-phytophagous (adults) insect also has no Se-dependent GPOX activity, although with increased age GSSG accumulation had been observed [20-221. Again, in relation to the aging process, a role of GSH peroxidase activity was argued for the fruitfly (Drosophilu rnelunoguster) [23]. A review of the assay (231, however, showed that the enzyme activity detected in D. rnelunoguster was actually due to a horseradish-like peroxidase (EC 1.11.1.7), which does not require GSH for activity [24], and this enzyme may have a role in the cuticular protein polymerization processes [25]. Thus, until recently there has been no evidence for the presence of Se-dependent GPOX enzyme in any insect examined.…”

Section: Introductionmentioning

confidence: 99%

Glutathione peroxidase activity in insects: A reassessment

Ahmad

Beilstein

Pardini

1989

Arch Insect Biochem Physiol

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In vertebrate species, cytotoxic H 2 0 2 and other lipid or organic hydroperoxides (ROOH) formed in aerobic metabolism are removed by a selenoprotein, glutathione peroxidase (GPOX). The GPOX activity in most rat tissues ranges from 100 to 1,000 units (1 unit = 1 nmol NADPH oxidized.mg protein-'.min-l), except for muscles (20-30 units). In contrast, GPOX activities of two strains of the housefly (Musca dornestica), cabbage looper (Eichoplusia ni), southern armyworm (Spodoptera eridania), and black swallowtail butterfly (fapilio polyxenes), were found to be in the range 2-12 units. Trivial GPOX activity was detected in the confused flour beetle (Eibolium confusurn). In the earthworm (Lumbricus terrestris), banana slug (Ariolirnax colurnbianus), and market squid (Loligo opalescens), the GPOX activity ranged from l to 5 units. Tissue selenium concentrations were about 500-1,000 ppb for adult M.dornestica, 600 ppb in T: confusurn, 32 ppb in T. ni, 17 ppb in S. eridania, and 31 ppb in F! polyxenes larvae. The form of selenium incorporated at such high levels in tissues of invertebrates such as M. dornestica remains an unresolved issue. Peroxidase activity of non-selenium glutathione-S-transferase (GT) against ROOH may compensate for the low GPOX activity. Catalase (CAT) has high activity and wide subcellular distribution in insects. This may be an evolutionary adaptation to GT's inability to catalyze the reduction of H 2 0 2 . The GT's peroxidase and CAT activities were not assessed for other invertebrate species, and warrants an investigation due to their reported low GPOX levels.

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“…7.14. This antioxidant function has been demonstrated for D. meianogaster, where the role of HRP was reported to surpass that of CAT (Armstrong et al, 1978;Nickla et al, 1983). In insects, HRP uses H20 2 and a number of phenolic substrates, o-catechols in particular, to form semiquinone radicals and quinones.…”

Section: Peroxidasementioning

confidence: 89%

Antioxidant Mechanisms of Enzymes and Proteins

Ahmad¹

1995

Oxidative Stress and Antioxidant Defenses in Biology

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Changes of peroxidase with age in drosophila

Cited by 39 publications

References 22 publications

Differential Activities of Antioxidant Enzymes, Superoxide Dismutase, Peroxidase, and Catalase vis-à-vis Phosphine Resistance in Field Populations of Lesser Grain Borer (Rhyzopertha dominica) from India

Differential Activities of Antioxidant Enzymes, Superoxide Dismutase, Peroxidase, and Catalase vis-à-vis Phosphine Resistance in Field Populations of Lesser Grain Borer (Rhyzopertha dominica) from India

Glutathione peroxidase activity in insects: A reassessment

Antioxidant Mechanisms of Enzymes and Proteins

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