scholarly journals Distribution of enzymes that catalyse reactions of glutathione with αβ-unsaturated compounds

1973 ◽  
Vol 131 (4) ◽  
pp. 765-769 ◽  
Author(s):  
L. F. Chasseaud
Keyword(s):  
Guinea Pig ◽  
Rat Liver ◽  
Rat Kidney ◽  
Acid Precipitation ◽  
Heat Inactivation ◽  
Phenoxyacetic Acid ◽  
Mercapturic Acids ◽  
Vertebrate Species ◽  
Methyl Vinyl

1. A study of the distribution of glutathione S-alkenetransferases in the livers of vertebrate species suggests that different enzymes may catalyse reactions of GSH with (i) trans-benzylideneacetone, (ii) 2,3-dimethyl-4(2-methylenebutyryl)phenoxyacetic acid, (iii) cinnamonitrile, (iv) o-chlorobenzylidenemalononitrile, (v) methyl vinyl sulphone, and (vi) 3-(β-nitrovinyl)indole. 2. Glutathione S-alkenetransferase activity was generally greatest in rat liver, but the enzyme in hamster liver was more active towards o-chlorobenzylidenemalononitrile, and the enzyme in rabbit, hamster, guinea-pig and mouse livers was more active towards methyl vinyl sulphone. 3. Results from studies of the distribution of activities in rat liver and rat kidney, heat inactivation of rat liver supernatants, and (NH4)2SO4 fractionation and acid-precipitation experiments, differentiated further between some of the enzymes concerned with substrates (i)–(vi). 4. The infrequent detection of mercapturic acids in vivo is discussed.

scholarly journals Glutathione S-aralkyltransferase

1969 ◽  
Vol 115 (5) ◽  
pp. 985-991 ◽  
Author(s):  
E. Boyland ◽  
L. F. Chasseaud
Keyword(s):  
Ammonium Sulphate ◽  
Rat Liver ◽  
Benzyl Chloride ◽  
Animal Species ◽  
Rat Kidney ◽  
Acid Precipitation ◽  
Heat Inactivation ◽  
Catalysed Reaction ◽  
Glutathione S Transferases ◽  
Ammonium Sulphate Fractionation

1. The name ‘glutathione S-aralkyltransferase’ is proposed for the enzyme catalysing the reaction of benzyl chloride with GSH. 2. Results from heat-inactivation studies, ammonium sulphate-fractionation and acid-precipitation experiments, and studies of the distribution of activities in rat liver, in rat kidney and in the livers of other animals indicate that glutathione S-aralkyltransferase differs from glutathione S-alkyltransferase, S-aryltransferase, S-epoxidetransferase and an S-alkenetransferase. 3. The distribution of these enzymes in the livers of the animal species examined was different. 4. Glutathione S-alkyltransferase, S-aralkyltransferase and the S-alkenetransferase that are present in rat liver supernatant were inhibited by GSSG, and the nature of the inhibition varied in each case. 5. 3,5-Di-tert.-butyl-4-hydroxybenzyl acetate reacts spontaneously with GSH, but the rat liver-supernatant-catalysed reaction of GSH with this and other aralkyl esters was weak. 6. A probable function of the glutathione S-transferases is the protection of cellular constituents from strong electrophilic agents.

scholarly journals Enzymes catalysing conjugations of glutathione with αβ-unsaturated carbonyl compounds

1968 ◽  
Vol 109 (4) ◽  
pp. 651-661 ◽  
Author(s):  
E. Boyland ◽  
L. F. Chasseaud
Keyword(s):  
Ammonium Sulphate ◽  
Carbonyl Compounds ◽  
Lower Energy ◽  
Rat Kidney ◽  
Heat Inactivation ◽  
Phenoxyacetic Acid ◽  
Diethyl Maleate ◽  
Catalysed Reaction ◽  
Ammonium Sulphate Fractionation ◽  
Inhibition Studies

1. Heat-inactivation experiments, ammonium sulphate-fractionation studies, enzyme-inhibition studies with S-(αβ-diethoxycarbonylethyl)glutathione, and evidence from the distribution of activities in rat liver, in rat kidney and in the livers of other animals, indicate that reactions of glutathione with (i) trans-benzylideneacetone, (ii) cyclohex-2-en-1-one, (iii) trans-cinnamaldehyde, (iv) diethyl maleate, (v) diethyl fumarate and (vi) 2,3-dimethyl-4-(2-methylenebutyryl)phenoxyacetic acid are catalysed by different enzymes. 2. Evidence is presented that the enzymes catalysing the reactions of glutathione with substrates (i)–(iv) are different from glutathione S-alkyltransferase, S-aryltransferase and S-epoxidetransferase. 3. The name ‘glutathione S-alkenetransferases’ is proposed for enzymes catalysing reactions of glutathione with αβ-unsaturated compounds. 4. The Arrenhius plot for the enzyme-catalysed reaction of diethyl maleate with glutathione is discontinuous, with lower energy of activation at 38°.

scholarly journals Molecular differences between rat-liver and rat-kidney biliverdin reductase. Implications for their in vivo regulation

1989 ◽  
Vol 179 (1) ◽  
pp. 123-130 ◽  
Author(s):  
Osvaldo CASCONE ◽  
Rosalia B. FRYDMAN ◽  
Pascual FERRARA ◽  
Maria L. TOMARO ◽  
Jorge ROSENFELD
Keyword(s):  
Rat Liver ◽  
Rat Kidney ◽  
Biliverdin Reductase

The Fine Structure of Rat Renal Microbodies and Cytoplasmic Bodies Following Perfusion Fixation

1973 ◽  
Vol 31 ◽  
pp. 620-621
Author(s):  
J. M. Barrett ◽  
P. M. Heidger
Keyword(s):  
Fine Structure ◽  
Proximal Tubule ◽  
Rat Kidney ◽  
Renal Proximal Tubule ◽  
Convincing Evidence ◽  
Cytoplasmic Bodies ◽  
Rat Renal Proximal Tubule ◽  
Renal Proximal Tubule Cells ◽  
Perfusion Fixation

Microbodies have received extensive morphological and cytochemical investigation since they were first described by Rhodin in 1954. To our knowledge, however, all investigations of microbodies and cytoplasmic bodies of rat renal proximal tubule cells have employed immersion fixation. Tisher, et al. have shown convincing evidence of fine structural alteration of microbodies in rhesus monkey kidney following immersion fixation; these alterations were not encountered when in vivo intravascular perfusion was employed. In view of these studies, and the fact that techniques for perfusion fixation have been established specifically for the rat kidney by Maunsbach, it seemed desirable to employ perfusion fixation to study the fine structure and distribution of microbodies and cytoplasmic bodies within the rat renal proximal tubule.

Inhibition of Human and Animal Platelet Adhesiveness to Glass Bead Columns by Adenosine, Dipyridamole, Chlorpromazine and Acetylsalicylic Acid

1976 ◽  
Vol 36 (02) ◽  
pp. 401-410 ◽  
Author(s):  
Buichi Fujttani ◽  
Toshimichi Tsuboi ◽  
Kazuko Takeno ◽  
Kouichi Yoshida ◽  
Masanao Shimizu
Keyword(s):  
Guinea Pig ◽  
Acetylsalicylic Acid ◽  
Guinea Pigs ◽  
Glass Bead ◽  
Animal Species ◽  
Inhibitory Effect ◽  
Rabbit Platelet ◽  
Platelet Adhesiveness

SummaryThe differences among human, rabbit and guinea-pig platelet adhesiveness as for inhibitions by adenosine, dipyridamole, chlorpromazine and acetylsalicylic acid are described, and the influence of measurement conditions on platelet adhesiveness is also reported. Platelet adhesiveness of human and animal species decreased with an increase of heparin concentrations and an increase of flow rate of blood passing through a glass bead column. Human and rabbit platelet adhesiveness was inhibited in vitro by adenosine, dipyridamole and chlorpromazine, but not by acetylsalicylic acid. On the other hand, guinea-pig platelet adhesiveness was inhibited by the four drugs including acetylsalicylic acid. In in vivo study, adenosine, dipyridamole and chlorpromazine inhibited platelet adhesiveness in rabbits and guinea-pigs. Acetylsalicylic acid showed the inhibitory effect in guinea-pigs, but not in rabbits.

Effect of X-irradiation on gene expression of rat liver chemokines: in vivo and in vitro studies

2008 ◽  
Vol 46 (01) ◽  
Author(s):  
F Moriconi ◽  
H Christiansen ◽  
H Christiansen ◽  
N Sheikh ◽  
J Dudas ◽  
...  
Keyword(s):  
Gene Expression ◽  
Rat Liver ◽  
In Vitro Studies ◽  
X Irradiation

Chronic, in vivo, PPARα activation prevents lipid overload in rat liver induced by high fat feeding

2009 ◽  
Vol 54 (1) ◽  
Author(s):  
M Wierzbicki ◽  
A Chabowski ◽  
M Żendzian-Piotrowska ◽  
E Harasim ◽  
J Górski
Keyword(s):  
Rat Liver ◽  
High Fat ◽  
Fat Feeding
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