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 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>.

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.

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.

scholarly journals The distribution, induction and isoenzyme profile of glutathione S-transferase and glutathione peroxidase in isolated rat liver parenchymal, Kupffer and endothelial cells

1989 ◽  
Vol 264 (3) ◽  
pp. 737-744 ◽  
Author(s):  
P Steinberg ◽  
H Schramm ◽  
L Schladt ◽  
L W Robertson ◽  
H Thomas ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Glutathione Peroxidase ◽  
Rat Liver ◽  
Peroxidase Activity ◽  
Cell Types ◽  
Transferase Activity ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Liver Parenchymal ◽  
Parenchymal Cells

The distribution and inducibility of cytosolic glutathione S-transferase (EC 2.5.1.18) and glutathione peroxidase (EC 1.11.1.19) activities in rat liver parenchymal, Kupffer and endothelial cells were studied. In untreated rats glutathione S-transferase activity with 1-chloro-2,4-dinitrobenzene and 4-hydroxynon-2-trans-enal as substrates was 1.7-2.2-fold higher in parenchymal cells than in Kupffer and endothelial cells, whereas total, selenium-dependent and non-selenium-dependent glutathione peroxidase activities were similar in all three cell types. Glutathione S-transferase isoenzymes in parenchymal and non-parenchymal cells isolated from untreated rats were separated by chromatofocusing in an f.p.l.c. system: all glutathione S-transferase isoenzymes observed in the sinusoidal lining cells were also detected in the parenchymal cells, whereas Kupffer and endothelial cells lacked several glutathione S-transferase isoenzymes present in parenchymal cells. At 5 days after administration of Arocolor 1254 glutathione S-transferase activity was only enhanced in parenchymal cells; furthermore, selenium-dependent glutathione peroxidase activity decreased in parenchymal and non-parenchymal cells. At 13 days after a single injection of Aroclor 1254 a strong induction of glutathione S-transferase had taken place in all three cell types, whereas selenium-dependent glutathione peroxidase activity remained unchanged (endothelial cells) or was depressed (parenchymal and Kupffer cells). Hence these results clearly establish that glutathione S-transferase and glutathione peroxidase are differentially regulated in rat liver parenchymal as well as non-parenchymal cells. The presence of glutathione peroxidase and several glutathione S-transferase isoenzymes capable of detoxifying a variety of compounds in Kupffer and endothelial cells might be crucial to protect the liver from damage by potentially hepatotoxic substances.

Expression of Glutathione S-Transferase Activity and Glutathione Content in Squamous Cell Carcinoma of Bladder Associated with Schistosomiasis in a Population in Egypt

1997 ◽  
Vol 31 (1) ◽  
pp. 43-47 ◽  
Author(s):  
Galal E. M. D. Ghazaly ◽  
Madeha M. Zakahary ◽  
Mohamed A. A. El-aziz ◽  
Ahmed A. E. M. Mahmoud ◽  
Pablo Carretero ◽  
...  
Keyword(s):  
Squamous Cell Carcinoma ◽  
Cell Carcinoma ◽  
Squamous Cell ◽  
Transferase Activity ◽  
Glutathione S Transferase
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