scholarly journals Sublethal effects of spinosad on some biochemical and biological parameters of Glyphodes pyloalis Walker (Lepidoptera: Pyralidae)

2014 ◽  
Vol 50 (No. 3) ◽  
pp. 135-144 ◽  
Author(s):  
F. Piri ◽  
A. Sahragard ◽  
M. Ghadamyari
Keyword(s):  
Enzyme Activity ◽  
Sublethal Effects ◽  
Protein A ◽  
Transferase Activity ◽  
Biological Parameters ◽  
Glutathione S Transferase ◽  
Female Fecundity ◽  
Significant Difference ◽  
Lepidoptera Pyralidae ◽  
Sublethal Concentrations

The susceptibility of G. pyloalis larvae to spinosad was studied using the leaf dip method. Treatment with doses of spinosad sublethal concentrations (LC<sub>10</sub>, LC<sub>20</sub>, LC<sub>30</sub>, LC<sub>40</sub> of 0.026, 0.045, 0.065, 0.090 ppm, respectively) was applied. A significant difference in the effects was observed between the sublethal concentrations (LC<sub>10</sub>, LC<sub>20</sub>, LC<sub>30</sub>, and LC<sub>40</sub>) and the control in the content of carbohydrate and glycogen, and between the control vs. LC<sub>30</sub> and LC<sub>40</sub> in the content of protein. A significant decrease in glutathione S-transferase activity with the increase of spinosad concentration, no significant differences in the activities of &alpha;- and &beta;-esterases, and a significant increase in the enzyme activity of phenoloxidase were observed. Effects of LC<sub>10</sub> and LC<sub>30</sub> spinosad concentrations on some biological parameters showed that percentage of larval pupation and female fecundity significantly decreased in the concentration of LC<sub>30</sub>.

Mechanisms of insecticide resistance in a temephos selected Culex quinquefasciatus (Diptera: Culicidae) strain from Sri Lanka

1990 ◽  
Vol 80 (4) ◽  
pp. 453-457 ◽  
Author(s):  
H.T.R. Peiris ◽  
J. Hemingway
Keyword(s):  
Cytochrome P450 ◽  
Sri Lanka ◽  
Culex Quinquefasciatus ◽  
Resistant Strain ◽  
Resistance Mechanism ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Biochemical Assays ◽  
Significant Difference ◽  
Naphthyl Acetate

AbstractCulex quinquefasciatus Say from Peliyagoda, Sri Lanka, has larval resistance to temephos, malathion, fenitrothion and chlorpyrifos. Biochemical assays on individual resistant and susceptible mosquitoes of this strain showed that there was a good correlation between this resistance and increased esterase activity with both 1-and 2-naphthyl acetate, which appears to be the major resistance mechanism in this multiple organophosphate resistant strain. There was no significant difference in malaoxon, bendiocarb or propoxur sensitivity of the acetylcholinesterase from the resistant and susceptible strains, indicating that the sensitivity of the target site has not been altered. Biochemical assays on mass homogenates of the resistant and susceptible strains showed no correlation between resistance and the level of glutathione s-transferase activity, or the amount of cytochrome P450 present.

scholarly journals A comparison of erythrocyte glutathione S-transferase activity from human foetuses and adults

1980 ◽  
Vol 188 (2) ◽  
pp. 475-479 ◽  
Author(s):  
R C Strange ◽  
J D Johnston ◽  
D R Coghill ◽  
R Hume
Keyword(s):  
Enzyme Activity ◽  
Catalytic Properties ◽  
Adult Life ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Human Foetuses

Glutathione S-transferase activity was measured in partially purified haemolysates of erythrocytes from human foetuses and adults. Enzyme activity was present in erythrocytes obtained between 12 and 40 weeks of gestation. The catalytic properties of the enzyme from foetal cells were similar to those of the enzyme from adult erythrocytes, indicating that probably only one form of the erythrocytes enzyme exists throughout foetal and adult life.

scholarly journals Identification of two lithocholic acid-binding proteins. Separation of ligandin from glutathione S-transferase B

1979 ◽  
Vol 181 (3) ◽  
pp. 699-708 ◽  
Author(s):  
J D Hayes ◽  
R C Strange ◽  
I W Percy-Robb
Keyword(s):  
Enzyme Activity ◽  
Binding Proteins ◽  
Peptide Mapping ◽  
Lithocholic Acid ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Liver Cytosol ◽  
Structural Differences ◽  
Distinct Subunit ◽  
Rat Liver Cytosol

1. Two lithocholic acid-binding proteins in rat liver cytosol, previously shown to have glutathione S-transferase activity, were resolved by CM-Sephadex chromatography. 2. Phenobarbitone administration resulted in induction of both binding proteins. 3. The two proteins had distinct subunit compositions indicating that they are dimers with mol.wts. 44 000 and 47 000. 4. The two lithocholic acid-binding proteins were identified by comparing their elution volumes from CM-Sephadex with those of purified ligandin and glutathione S-transferase B prepared by published procedures. Ligandin and glutathione S-transferase B were eluted separately, as single peaks of enzyme activity, at volumes equivalent to the two lithocholic acid-binding proteins. 5. Peptide ‘mapping’ revealed structural differences between the two proteins.

Urinary Ligandin and Glutathione-S-Transferase in Gentamicin-Induced Nephrotoxicity in the Rat

1981 ◽  
Vol 61 (1) ◽  
pp. 123-125 ◽  
Author(s):  
D. A. Feinfeld ◽  
G. M. Fleischner ◽  
I. M. Arias
Keyword(s):  
Enzyme Activity ◽  
Serum Creatinine ◽  
Transferase Activity ◽  
Tubular Injury ◽  
Glutathione S Transferase ◽  
Proximal Tubular ◽  
Renal Proximal Tubular

1. Eight rats developed detectable glutathione-S-transferase activity in their urine after three daily injections of toxic doses of gentamicin. 2. Seven of the eight rats had immunodetectable ligandin in their urine at this time. 3. The level of enzyme activity correlated well with the degree of elevation of serum creatinine. 4. This confirms ligandinuria and urinary glutathione-S-transferase as markers of acute renal proximal tubular injury.

Characteristics of Insulin-degrading Enzyme in Alzheimer's Disease: A Meta-Analysis

2018 ◽  
Vol 15 (7) ◽  
pp. 610-617 ◽  
Author(s):  
Huifeng Zhang ◽  
Dan Liu ◽  
Huanhuan Huang ◽  
Yujia Zhao ◽  
Hui Zhou
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Enzyme Activity ◽  
Protein Level ◽  
Senile Plaque ◽  
Meta Analysis ◽  
Cochrane Library ◽  
Insulin Degrading Enzyme ◽  
Degrading Enzyme ◽  
Significant Difference

Background: β-amyloid (Aβ) accumulates abnormally to senile plaque which is the initiator of Alzheimer's disease (AD). As one of the Aβ-degrading enzymes, Insulin-degrading enzyme (IDE) remains controversial for its protein level and activity in Alzheimer's brain. Methods: The electronic databases PubMed, EMBASE, The Cochrane Library, OVID and Sinomed were systemically searched up to Sep. 20th, 2017. And the published case-control or cohort studies were retrieved to perform the meta-analysis. Results: Seven studies for IDE protein level (AD cases = 293; controls = 126), three for mRNA level (AD cases = 138; controls = 81), and three for enzyme activity (AD cases = 123; controls = 75) were pooling together. The IDE protein level was significantly lower in AD cases than in controls (SMD = - 0.47, 95% CI [-0.69, -0.24], p < 0.001), but IDE mRNA and enzyme activity had no significant difference (SMD = 0.02, 95% CI [-0.40, 0.43] and SMD = 0.06, 95% CI [-0.41, 0.53] respectively). Subgroup analyses found that IDE protein level was decreased in both cortex and hippocampus of AD cases (SMD = -0.43, 95% CI [-0.71, -0.16], p = 0.002 and SMD = -0.53, 95% CI [-0.91, -0.15], p = 0.006 respectively). However, IDE mRNA was higher in cortex of AD cases (SMD = 0.71, 95% CI [0.14, 1.29], p = 0.01), not in hippocampus (SMD = -0.26, 95% CI [-0.58, 0.06]). Conclusions: Our results indicate that AD patients may have lower IDE protease level. Further relevant studies are still needed to verify whether IDE is one of the factors affecting Aβ abnormal accumulation and throw new insights for AD detection or therapy.

scholarly journals Sublethal effects of emamectin benzoate on life table parameters of the cotton leafworm, Spodoptera littoralis (Boisd.)

2020 ◽  
Vol 44 (1) ◽  
Author(s):  
El-Sayed Mokbel ◽  
Amal Huesien
Keyword(s):  
Life Table ◽  
Spodoptera Littoralis ◽  
Sublethal Effects ◽  
Lethal Effect ◽  
Reproductive Rate ◽  
Relative Fitness ◽  
Emamectin Benzoate ◽  
Cotton Leafworm ◽  
Sublethal Concentrations ◽  
Preovipositional Period

Abstract Background The cotton leafworm, Spodoptera littoralis (Boisd.), is a serious economic pest in Egypt. Pest control depends mainly on chemical control with several pesticides include conventional and modern insecticides. Comprehensive analysis of pesticides impacts needs to investigate sublethal effects in addition to lethal effect. Results In the current study, the leaf-dip bioassay method was used to evaluate emamectin benzoate (EMB) sublethal concentrations. Results showed that EMB proved high toxicity against S. littorals with LC50 value of 0.019 mg liter−1. Life table analysis showed that treatments with LC5 and LC15 prolonged larval period, mean longevity of males and females, mean generation time (T), doubling time (DT), adult preovipositional period (APOP), and total preovipositional period (TPOP) compared with control. On the contrary, net reproduction rates (R0), intrinsic rates of increase (r), finite rate (λ), fecundity, gross reproductive rate (GRR), and relative fitness were decreased compared to control. Conclusions The current study clarified that sublethal concentrations of EMB induce adverse effects and suppress the population growth of S. littorals. Our results would be useful to assess the overall effects of EMB on S. littorals and can contribute effectively in pest management.

Antioxidant Enzyme Levels Inversely Covary with Hearing Loss After Amikacin Treatment

2003 ◽  
Vol 14 (03) ◽  
pp. 134-143 ◽  
Author(s):  
James J. Klemens ◽  
Robert P. Meech ◽  
Larry F. Hughes ◽  
Satu Somani ◽  
Kathleen C.M. Campbell
Keyword(s):  
Hearing Loss ◽  
Enzyme Activity ◽  
Antioxidant Enzyme ◽  
Guinea Pigs ◽  
Auditory Brainstem ◽  
Antioxidant Enzyme Activity ◽  
Control Group ◽  
Glutathione S Transferase ◽  
Brainstem Response ◽  
The Difference

This study's purpose was to determine if a correlation exists between cochlear antioxidant activity changes and auditory function after induction of aminoglycoside (AG) ototoxicity. Two groups of five 250-350 g albino guinea pigs served as subjects. For 28 days, albino guinea pigs were administered either 200 mg/kg/day amikacin, or saline subcutaneously. Auditory brainstem response testing was performed prior to the first injection and again before sacrifice, 28 days later. Cochleae were harvested and superoxide dismutase, catalase, glutathione peroxidase, glutathione-S-transferase, glutathione reductase activities and malondialdehyde levels were measured. All antioxidant enzymes had significantly lower activity in the amikacin group (p ≤ 0.05) than in the control group. The difference in cochlear antioxidant enzyme activity between groups inversely correlated significantly with the change in ABR thresholds. The greatest correlation was for the high frequencies, which are most affected by aminoglycosides. This study demonstrates that antioxidant enzyme activity and amikacin-induced hearing loss significantly covary.

Glutathione S-Transferase Activity in Nontreated and CGA-154281- Treated Maize Shoots

1991 ◽  
Vol 46 (9-10) ◽  
pp. 850-855 ◽  
Author(s):  
John V. Dean ◽  
John W. Gronwald ◽  
Michael P. Anderson
Keyword(s):  
Liquid Chromatography ◽  
Anion Exchange ◽  
Cinnamic Acid ◽  
Fast Protein Liquid Chromatography ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Selective Enhancement

Abstract Fast protein liquid chromatography (anion exchange) was used to separate glutathione S-transferase isozymes in nontreated etiolated maize shoots and those treated with the herbi­cide safener CGA -1542814-(dichloroacetyl)-3,4-dihydro-3-methyl-2 H-1 ,4-benzoxazine. Non­treated shoots contained isozymes active with the following substrates: trans-cinnamic acid (1 isozyme), atrazine (3 isozymes), 1-chloro-2,4-dinitrobenzene (1 isozyme), metolachlor (2 isozymes) and the sulfoxide derivative of S-ethyl dipropylcarbamothioate (2 isozymes). Pre­treatment of shoots with the safener CGA -154281 (1 μM) had no effect on the activity of the isozymes selective for trans-cinnamic acid and atrazine but increased the activity of the constitutively-expressed isozymes that exhibit activity with 1-chloro-2,4-dinitrobenzene, metola­chlor and the sulfoxide derivative of S-ethyl dipropylcarbamothioate. The safener pretreat­ment also caused the appearance of one new isozyme active with 1-chloro-2,4-dinitrobenzene and one new isozyme active with metolachlor. The results illustrate the complexity of gluta­thione S-transferase activity in etiolated maize shoots, and the selective enhancement of gluta­thione S-transferase isozymes by the safener CGA -154281.

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