scholarly journals Alcohol Dehydrogenase- and Rat Liver Cytosol-Dependent Bioactivation of 1-Chloro-2-hydroxy-3-butene to 1-Chloro-3-buten-2-one, a Bifunctional Alkylating Agent

2012 ◽  
Vol 25 (11) ◽  
pp. 2600-2607 ◽  
Author(s):  
Adnan A. Elfarra ◽  
Xin-Yu Zhang
Keyword(s):  
Alcohol Dehydrogenase ◽  
Rat Liver ◽  
Alkylating Agent ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals 4-Hydroxy-2(E)-nonenal enantiomers: (S)-selective inactivation of glyceraldehyde-3-phosphate dehydrogenase and detoxification by rat glutathione S-transferase A4-4

2000 ◽  
Vol 349 (3) ◽  
pp. 729-735 ◽  
Author(s):  
Akira HIRATSUKA ◽  
Kenichiro HIROSE ◽  
Hiroshi SAITO ◽  
Tadashi WATABE
Keyword(s):  
Lipid Peroxidation ◽  
Alcohol Dehydrogenase ◽  
Rat Liver ◽  
Catalytic Efficiency ◽  
Glycolytic Enzyme ◽  
Glutathione S Transferase ◽  
Liver Cytosol ◽  
Mediated Reduction ◽  
Rat Liver Cytosol ◽  
In Cells

The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase was irreversibly and (S)-selectively inactivated by the enantiomers of racemic 4-hydroxy-2(E)-nonenal (HNE), a reactive product released from biomembranes by lipid peroxidation in cells. Rates of the enzyme inactivations were 1.7, 3.0, and 6.0M-1·s-1 for (R)-, racemic and (S)-HNEs respectively. In rat liver cytosol the HNE was detoxified 2.5-fold more (S)-selectively by GSH conjugation and 2.4-fold more (R)-selectively by NADH-dependent reduction mediated by alcohol dehydrogenase (ADH) than the opposite enantiomers. However, in the cytosol the GSH conjugation of (R)-HNE proceeded at a much higher rate than did its ADH-mediated reduction. The minor glutathione S-transferase (GST) isoform, A4-4, in the rat (r) liver had a major role in the cytosolic (S)-selective GSH conjugation. The catalytic efficiency, kcat/Km, of purified rGSTA4-4 was 4-fold higher for (S)-HNE than for (R)-HNE; the Km was 3-fold higher for (R)-HNE than for (S)-HNE. (S)-HNE was preferentially detoxified to (R)-HNE by rGSTA4-4 when racemic HNE was used as a substrate.

scholarly journals Alterations in translatable messenger RNA coding for phosphoenolpyruvate carboxykinase (GTP) in rat liver cytosol during deinduction.

1978 ◽  
Vol 253 (12) ◽  
pp. 4327-4332
Author(s):  
D. Kioussis ◽  
L. Reshef ◽  
H. Cohen ◽  
S.M. Tilghman ◽  
P.B. Iynedjian ◽  
...  
Keyword(s):  
Rat Liver ◽  
Messenger Rna ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals Transformation of the glucocorticoid receptor in rat liver cytosol by lysosomal enzymes.

1979 ◽  
Vol 254 (5) ◽  
pp. 1537-1539 ◽  
Author(s):  
J. Carlstedt-Duke ◽  
O. Wrange ◽  
E. Dahlberg ◽  
J.A. Gustafsson ◽  
B. Högberg
Keyword(s):  
Glucocorticoid Receptor ◽  
Rat Liver ◽  
Lysosomal Enzymes ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

Development of an [3H] glucocorticoid exchange assay in rat liver cytosol

Steroids ◽  
1981 ◽  
Vol 37 (4) ◽  
pp. 409-421 ◽  
Author(s):  
Ashutosh Banerji ◽  
Mohammed Kalimi
Keyword(s):  
Rat Liver ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

scholarly journals Rat liver cytosol oxysterol-binding protein

FEBS Letters ◽  
1987 ◽  
Vol 210 (1) ◽  
pp. 97-103 ◽  
Author(s):  
F. Beseme ◽  
M.E. Astruc ◽  
R. Defay ◽  
A.Crastes de Paulet
Keyword(s):  
Rat Liver ◽  
Binding Protein ◽  
Liver Cytosol ◽  
Oxysterol Binding Protein ◽  
Rat Liver Cytosol
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