scholarly journals Purification and properties of anionic glutathione S-transferase from bovine ciliary body

1986 ◽  
Vol 237 (2) ◽  
pp. 365-371 ◽  
Author(s):  
H Shichi ◽  
P D O'Meara
Keyword(s):  
Amino Acid ◽  
Glutathione Peroxidase ◽  
Ciliary Body ◽  
Competitive Inhibitor ◽  
Transferase Activity ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Substrate Specificities ◽  
Purification And Properties ◽  
Peptide Maps

An anionic glutathione S-transferase was purified from bovine ciliary body by DEAE-agarose chromatography and affinity chromatography on GSH-agarose and Orange A. The enzyme accounts for about 25% of total soluble glutathione S-transferase activity of the tissue. The purified enzyme has a molecular mass of about 50,000 Da and is composed of two identical subunits of about 25,000 Da. The enzyme has a pI of 5.8. The enzyme conjugates GSH with 1-chloro-2,4-dinitrobenzene, p-nitrobenzyl chloride, 1,2-epoxy-3-(p-nitrophenyl)propane, 1,2-dinitrobenzene and 3,4-dinitrobenzoic acid. The Km values for 1-chloro-2,4-dinitrobenzene and GSH are 0.40 mM and 0.57 mM respectively. Haematin is a non-competitive inhibitor (Ki = 4.5 microM) when tested with various concentrations of 1-chloro-2,4-dinitrobenzene. The enzyme shows no glutathione peroxidase activity with either H2O2 or cumene peroxide as substrate. On the basis of substrate specificities, pI values, amino acid composition and peptide maps, it is concluded that the ciliary-body enzyme is probably identical with the anionic form of glutathione S-transferase from bovine lens and liver.

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.

Microsomal glutathione S-transferase A1-1 with glutathione peroxidase activity from sheep liver: molecular cloning, expression and characterization

2001 ◽  
Vol 360 (2) ◽  
pp. 345-354 ◽  
Author(s):  
K. Sandeep PRABHU ◽  
Padala V. REDDY ◽  
Eric GUMPRICHT ◽  
George R. HILDENBRANDT ◽  
Richard W. SCHOLZ ◽  
...  
Keyword(s):  
Amino Acid ◽  
Glutathione Peroxidase ◽  
Molecular Mass ◽  
Peroxidase Activity ◽  
Sequence Similarity ◽  
Liver Microsomes ◽  
Amino Acid Residues ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Sheep Liver

A 25kDa subunit of glutathione S-transferase (GST) from sheep liver microsomes (microsomal GSTA1-1) with a significant selenium-independent glutathione peroxidase activity has been isolated and characterized. Several analytical criteria, including EDTA stripping, protease protection assay and extraction with alkaline Na2CO3, indicate that the microsomal GSTA1-1 is associated with the inner microsomal membrane. The specific cDNA nucleotide sequence reveals that the enzyme is made up of 222 amino acid residues and shares approx. 73–83% sequence similarity to Alpha-class GSTs from different species. The molecular mass, as determined by electrospray mass ionization, is 25611.3Da. The enzyme is distinct from the previously reported rat liver microsomal GST in both amino acid sequence and catalytic properties [Morgenstern, Guthenberg and DePierre (1982) Eur. J. Biochem. 128, 243–248]. The microsomal GSTA1-1 differs from the sheep liver cytosolic GSTs, reported previously from this laboratory, in its substrate specificity profile and molecular mass [Reddy, Burgess, Gong, Massaro and Tu (1983) Arch. Biochem. Biophys. 224, 87–101]. In addition to catalysing the conjugation of 4-hydroxynonenal with GSH, the enzyme also exhibits significant glutathione peroxidase activity towards physiologically relevant fatty acid hydroperoxides, such as linoleic and arachidonic acid hydroperoxides, as well as phosphatidylcholine hydroperoxide, but not with H2O2. Thus the microsomal GSTA1-1 isoenzyme might have an important role in the protection of biological membranes against oxidative damage.

scholarly journals The influence of melatonin on the state of the glutathione system of the rat liver under the conditions of subacute alcoholic intoxication

2014 ◽  
Vol 18 (3 (71)) ◽  
Author(s):  
N. V. Davydova
Keyword(s):  
Glutathione Peroxidase ◽  
Oral Administration ◽  
Rat Liver ◽  
Peroxidase Activity ◽  
Reduced Glutathione ◽  
Alcohol Intoxication ◽  
Transferase Activity ◽  
Glutathione System ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase

The investigations of certain parameters of glutathione system in the liver of rats under the conditions of subacute alcohol intoxication revealed a decreased content of reduced glutathione and glutathione peroxidase activity as well as an activation of glutathione-S-transferase activity. An oral administration of “Vita-melatonin” against a background of subacute alcohol intoxication in a dose 5 mg/kg during 10 days prevented the changes of the parameters under study.

scholarly journals Antioxidants in erythrocytes in aging and dementia

2013 ◽  
Vol 59 (4) ◽  
pp. 443-451 ◽  
Author(s):  
E.A. Kosenko ◽  
L.A. Tikhonova ◽  
A.C. Poghosyan ◽  
Y.G. Kaminsky
Keyword(s):  
Oxidative Stress ◽  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Glutathione Peroxidase ◽  
Antioxidant Status ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Age Related ◽  
Organic Hydroperoxides

Age of patients and brain oxidative stress may contribute to pathogenesis of Alzheimer's disease (AD). Erythrocytes (red blood cells, RBC) are considered as passive “reporter cells” for the oxidative status of the whole organism and are not well studied in AD. The aim of this work was to assess whether the antioxidant status of RBC changes in aging and AD. Blood was taken from AD and non-Alzheimer's dementia patients, aged-matched and younger controls. In vivo antioxidant status was assessed in each of the study subjects by measuring RBC levels of Н О , organic hydroperoxides, glutathione (GSH) and glutathione disulfide (GSSG), activities of superoxide dismutase, catalase, glutathione peroxidase, glutathione reductase, glutathione S-transferase, and glucose-6-phosphate dehydrogenase. In both aging and dementia, oxidative stress in RBC was shown to increase and to be expressed in elevated concentrations of H O and organic hydroperoxides, decreased the GSH/GSSG ratio and glutathione S-transferase activity. Decreased glutathione peroxidase activity in RBC may be considered as a new peripheral marker for Alzheimer’s disease while alterations of other parameters of oxidative stress reflect age-related events.

The effect of dietary protein and sulfur amino acids on hepatic glutathione concentration and glutathione-dependent enzyme activities in the rat

1988 ◽  
Vol 66 (8) ◽  
pp. 1048-1052 ◽  
Author(s):  
P. F. Bauman ◽  
T. K. Smith ◽  
T. M. Bray
Keyword(s):  
Amino Acids ◽  
Glutathione Peroxidase ◽  
Glutathione Reductase ◽  
Dietary Protein ◽  
Transferase Activity ◽  
Sulfur Amino Acids ◽  
Glutathione S Transferase ◽  
Glutathione Concentration ◽  
Hepatic Glutathione ◽  
Protein Diets

Hepatic glutathione concentration and glutathione-dependent enzymes, glutathione S-transferase, glutathione peroxidase, and glutathione reductase, are important for protection against toxic compounds. Rats were fed diets containing 4, 7.5, 15, or 45% protein for 2 weeks. Glutathione and cysteine concentrations in rats fed the 4 and 7.5% protein diets were significantly lower (p < 0.05) than in rats fed the 15 and 45% protein diets. Glutathione S-transferase activity increased with increasing dietary protein. Glutathione peroxidase activity was significantly lower (p < 0.05) in rats fed 4 and 7.5% protein compared with rats fed 15 and 45% protein, whereas the activity of glutathione reductase was higher in rats fed 4 and 7.5% protein then in rats fed 15 or 45% protein. Dietary sulfur amino acids alone could account for the increase in glutathione concentration resulting from the increase in dietary protein from 7.5 to 15%. The limited availability of glutathione in animals fed the low protein diets could reduce the potential for detoxification of xenobiotics.

Effect of abiotic stresses on glutathione peroxidase and glutathione S-transferase activity in barley root tips

2009 ◽  
Vol 47 (11-12) ◽  
pp. 1069-1074 ◽  
Author(s):  
L’ubica Halušková ◽  
Katarína Valentovičová ◽  
Jana Huttová ◽  
Igor Mistrík ◽  
Ladislav Tamás
Keyword(s):  
Glutathione Peroxidase ◽  
Abiotic Stresses ◽  
Barley Root ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Root Tips

scholarly journals Interrelationship between cationic and anionic forms of glutathione S-transferases of bovine ocular lens

1980 ◽  
Vol 191 (1) ◽  
pp. 11-20 ◽  
Author(s):  
R P Saneto ◽  
Y C Awasthi ◽  
S K Srivastava
Keyword(s):  
Amino Acid ◽  
Glutathione Peroxidase ◽  
Vascular System ◽  
Liver Homogenate ◽  
Physiological Role ◽  
Antigenic Determinants ◽  
Ocular Lens ◽  
Glutathione S Transferase ◽  
Amino Acid Compositions ◽  
Bovine Lens

Since the eye is constantly exposed to potentially damaging chemical compounds present in the atmosphere and vascular system, we investigated the physiological role of glutathione S-transferase (GSH S-transferase) in detoxification mechanisms operative in the ocular lens. We have purified an anionic and a cationic GSH S-transferase from the bovine lens to homogeneity through a combination of gel filtration, ion-exchange and affinity chromatography. The anionic (pI 5.6) and cationic (pI 7.4) S-transferases were found to have distinct kinetic parameters (apparent Km and Vmax. pH optimum and energy of activation). However, both species were demonstrated to have similar molecular weights and amino acid compositions. Double-immunodiffusion and immunotitration studies showed that both lens S-transferases were immunologically similar. The very close similarity in amino acid compositions and immunological properties strongly indicates that these two transferases either originate from the same gene or at least share common antigenic determinants and originate from similar genes. The bovine lens GSH S-transferases had no glutathione peroxidase activity with either t-butyl hydroperoxide or cumene hydroperoxide as substrate. However, the antibody raised against the homogeneous anionic glutathione S-transferase from the bovine lens was found to precipitate both glutathione S-transferase and glutathione peroxidase activities out of solution in the supernatant of a crude bovine liver homogenate.

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